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Lotte Hotels & Resorts
The company was founded in 1973.
Fuerte Hotels
Fuerte Hotels is a hotel chain primarily based in Andalusia; Costa del Sol, Costa de la Luz & Sierra de Grazalema in (Spain).
Home2 Suites by Hilton
Home2 Suites by Hilton is a mid-tier, all-suite extended-stay hotel featuring contemporary accommodations and customizable guest room design.
Bahia Principe
The company currently maintains a total of 24 five-star beach resorts: in Palma de Mallorca and Tenerife (Spain); Riviera Maya (Mexico); Samaná, La Romana, Punta Cana, and Puerto Plata (Dominican Republic); and Runaway Bay(Jamaica).
Radisson Blu
Radisson Blu (formerly Radisson SAS) is an upscale international chain of full service hotels and resorts brand for Radisson Hotels mostly outside the United States, including those in Europe, Africa, and Asia.
Red Lion Hotels Corporation
Red Lion Hotels Corporation is a US hospitality corporation that primarily engages in the franchising, management and ownership of upscale, midscale and economy hotels.
Tsokkos Hotels (CY: TSH) is a hotel chain owned by the Tsokkos family.
Umi hotels
umi Hotels is a budget hotel chain based in Leinster Square in Bayswater, London.
B&B Hotels
B&B Hotels is a hotel chain started in Brittany, France in 1990.
W Hotels
W Hotels & Resorts is a luxury hotel chain owned by Starwood Hotels & Resorts Worldwide that is generally marketed toward a younger crowd than their other upscale properties.
Pierre & Vacances
Groupe Pierre & Vacances Center Parcs (French pronunciation: [ɡʁup pjɛʁ e vakɑ̃s sɑ̃te paʁks]) specializes in tourism services, providing holiday and entertainment villages, leisure activity residences and hotels under the brands Pierre & Vacances, Maeva, Center Parcs, Sunparks, and Adagio (the last in partnership with Accor).
Relais & Châteaux
Relais & Châteaux is a global fellowship of individually owned and operated luxury hotels and restaurants.
Rocco Forte Hotels
Rocco Forte Hotels is a group of luxury hotels and resorts.
Taj Hotels Resorts and Palaces
Indian Hotels Company Limited (IHCL), branded as Taj Hotels Resorts and Palaces, is a chain of hotels and resorts headquartered at Oxford House in Mumbai, which was incorporated by the founder of the Tata group, Jamsetji Tata, in the year 1903.
The LaLiT Hotels, Palaces and Resorts
The LaLiT Hotels is the flagship brand of Bharat Hotels Limited Enterprise, a part of The LaLiT Suri Hospitality Group.
Mercure Hotels
Mercure Hotels is a brand of hotels run by French multinational corporation AccorHotels.
Virgin Hotels
Virgin Hotels is a brand of hotels created by Sir Richard Branson's Virgin Group, launched in 2010.
Renaissance Hotels
Renaissance Hotels is a worldwide brand of hotels and resorts.
Mielparque (メルパルク Meruparuku) is a Japanese hotel chain.
Mövenpick Hotels & Resorts
Mövenpick Hotels & Resorts (German pronunciation: [ˈmœːvənˌpɪk]; English /ˈmuːvənˌpɪk/) is a hotel management company headquartered in Baar, Switzerland.
Morgans Hotel Group
Morgans Hotel Group (MHG) is a hospitality company that owns & operates boutique hotels, as well as acquiring and redeveloping in the United States and Europe.
Mandarin Oriental Hotel Group
Mandarin Oriental Hotel Group (MOHG) (Traditional Chinese: 文華東方酒店), a member of the Jardine Matheson Group, is a British international hotel investment and management group with luxury hotels, resorts and residences in Asia, Europe and the Americas.
NH Hotel Group
NH Hotel Group (officially NH Hotel Group SA, BMAD: NHH) is a Spanish-based hotel chain headquartered in Madrid.
Nylo Hotels
NYLO Hotels LLC is an American boutique hotel chain.
Ace Hotel
Ace Hotel is a chain of hotels headquartered in Portland, Oregon.
Aerowisata is an Indonesian hospitality company based in Jakarta.
Outrigger Hotels & Resorts
Outrigger Hotels is a Honolulu-based hotel chain and management company operating a multi-branded line of hotels, condominiums and vacation resort properties in Hawaii and the Asia-Pacific region.
Peppermint Hotels
Peppermint Hotels is an Indian budget boutique hotel chain.
Courtyard by Marriott
Courtyard by Marriott is a brand of hotels owned by Marriott International.
Go Hotels
Go Hotels is a chain of budget hotels in the Philippines.
Center Parcs
Center Parcs is a European network of holiday villages.
Embassy Suites by Hilton
Embassy Suites by Hilton is a chain of upscale all-suite hotels trademarked by Hilton Worldwide.
Even Hotels
Even Hotels (styled EVEN Hotels) is a hotel brand concept created by InterContinental Hotels Group in 2012 to create a hotel that meets travelers' holistic wellness needs.
Fairfield Inn by Marriott
Fairfield Inn by Marriott is a lower-cost, economy brand of hotels that are franchised by Marriott International.
GreenTree Inns
GreenTree Inns Hotel Management Group, Inc.
Baglioni Hotels
Baglioni Hotels is an Italian company that owns a chain of 9 extra luxury hotels, most of which are situated in palazzos in Italy's main cities: six in Italy (Milan, Venice, Florence, Punta Ala and Rome), three in France (Aix-en-Provence, Champillon Epernay, Saint Paul de Vence) and one established in March 2004 in the UK, in the heart of London.
Jetwing Hotels
Jetwing Hotels Limited is a Sri Lankan hotel chain.
Curio (brand)
Curio – A Collection by Hilton is a luxury hotel brand part of Hilton Worldwide's portfolio.
Tru by Hilton
Tru by Hilton is a brand of hotels trademarked by Hilton Worldwide.
Travelodge Australia
Travelodge Hotels is an Australian hotel chain operated by TFE Hotels offering accommodation across 17 locations in Australia and New Zealand.
The Davenport Hotel Collection
The Davenport Hotel Collection is a brand collection of four upscale hotels in Spokane, Washington.
Okura Hotels
Okura Hotels & Resorts (オークラ ホテルズ & リゾーツ) is a hotel chain with locations mainly in Japan.
Adagio (hotel)
Adagio City Aparthotel is a joint venture launched by Accor Hotels and Pierre & Vacances, and is a major hotel company proposing a formula of apartments for rent in large cities, responding to changing needs.
JW Marriott Hotels
JW Marriott Hotels & Resorts, namesake of John Willard Marriott, Founder, Chairman & CEO of Marriott International is a luxury hotel chain.
Hoshino Resorts
Hoshino Resort Co.
Hilton Garden Inn
Hilton Garden Inn is a chain of upscale, mid-priced hotels trademarked by Hilton Worldwide.
Fairmont Hotels and Resorts
Fairmont Hotels & Resorts is a Canadian operator of luxury hotels and resorts.
Autograph Collection Hotels
Autograph Collection Hotels is a luxury hotel chain owned by Marriott International.
Motel 6
Motel 6 is a chain of budget motels in the United States and Canada.
Couples Resorts
Couples Resorts was the very first resort to use the "all-inclusive" resort concept to open in the Caribbean.
Omni Hotels & Resorts
Omni Hotels & Resorts is an American privately held, international luxury hotel company based in Dallas, Texas.
Principal Hayley Group
Principal Hayley Group is a British hotel and conference venue operator whose headquarters are in Harrogate in North Yorkshire.
Principe di Savoia
Hotel Principe di Savoia, or simply referred to as The Principe, is a five-star hotel in Milan, Italy.
Jurys Inn
Jurys Inns is a chain of hotels founded in Ireland and previously owned by Jurys Doyle Hotel Group.
Pullman Hotels and Resorts
Pullman Hotels and Resorts is an upscale international hotel brand owned by AccorHotels.
Grupo Habita
Grupo Habita is a boutique hotel developer-operator based in Mexico City that owns hotels across Mexico and several in the United States.
Red Planet Hotels
Red Planet Hotels is a privately owned regional hotel company founded in 2010 that focuses on Asia's expanding value hotel sector.
Lark Hotels
Lark Hotels is a hotel management and development company, which owns and develops hotels, mostly in New England.
Minor Hotels
(See also: Minor International) Minor Hotel Group (MHG) is a hotel owner, operator, and investor.
Banyan Tree Holdings
Banyan Tree Holdings Limited is an international hospitality brand that manages and develops resorts, hotels and spas in Asia, America, Africa and Middle East.
Cobblestone Hotels
Cobblestone Hotels is a chain of hotels in the United States.
The Hoxton
The Hoxton is an international hotel chain owned by Ennismore.
Starhotels is a privately owned hotel chain based in Florence that operates 24 luxury hotels (20 in Italy, 2 in London, and one each in Paris and New York City).
Baymont Inn & Suites
Baymont Inn & Suites is a hotel franchise owned by Wyndham Worldwide and based in the United States.
Mamaison Hotels & Residences is a collection of 8 midscale to upscale hotels and residences.
Mondrian Hotel
Mondrian Hotels is the name of four boutique hotels owned and/or operated by the Morgans Hotel Group.
RockResorts is a hotel brand with roots in the 1950s.
The Plaza Hotel Seoul
THE PLAZA is a South Korean operator of hotels and is affiliated to Preferred Hotels & Resorts, the top level of the six brands of Preferred Hotel Group.
Leading Hotels of the World, Ltd
The company was established in 1928 under the name "Luxury Hotels of Europe and Egypt".
Langham Hospitality Group
Langham Hospitality Group is a luxury hotels operator dating back to 1865, when The Langham, London originally opened as Europe's first 'Grand Hotel'.
MKG Group
MKG Group is a European-based company, headquartered in Paris, France.
Magnuson Hotels
Magnuson Hotels is an American hotel chain & affiliate.
Budget Host
Budget Host is an American lodging chain.
Groupe Lucien Barrière
Groupe Lucien Barrière operates casinos in France, Switzerland and elsewhere in Europe.
Dorchester Collection
Dorchester Collection is a luxury hotel operator owned by the Brunei Investment Agency (BIA), an arm of the Ministry of Finance of Brunei.
Drury Hotels
Drury Hotels, LLC is an American hospitality company which operates a chain of mid-scale limited service hotels under the brands Drury Inn and Suites (its flagship brand), Drury Inn, Drury Suites, Drury Plaza Hotel, and Pear Tree Inn.
Rydges Hotels & Resorts
Rydges Hotels & Resorts, or Rydges, is a hotel accommodation and hospitality provider that operates in Australia and New Zealand, and in the city of London, England.
Abu Dhabi National Hotels
Abu Dhabi National Hotels is broad based hotel, tourism, transport and catering group, part of which is owned by the Abu Dhabi government.
Days Inns – Canada
Days Inns – Canada is a hotel chain with 100 independently owned and operated properties and over 8,600 rooms.
AC Hotels
AC Hotels by Marriott owns and operates a chain of hotels in Brazil, Denmark, France, Italy, Portugal, Spain, Turkey and North America.
Hotel Grand Chancellor
Hotel Grand Chancellor is a hotel chain that operates throughout Australia and New Zealand.
Howard Johnson's
Howard Johnson's, or Howard Johnson, is a chain of hotels, motels and restaurants located primarily throughout the United States and Canada.
Marco Polo Hotels
Marco Polo Hotels (Chinese: 馬哥孛羅酒店集團) is a hotel management company based in Hong Kong that operates hotels in Hong Kong, China and the Philippines.
Imperial Hotels Group
Imperial Hotels Group is a hotel conglomerate, based in Uganda, with operations in Kampala and Entebbe.
Divan Group
Divan Group is a hotel group based in Turkey; its flagship is the Divan Istanbul next to Taksim Gezi Park.
Sofitel is a French hotel chain under AccorHotels, which opened its first property in Strasbourg in 1964.
Shilo Inns
Shilo Inns is a mid-priced hotel chain operating 31 hotels predominantly on the west coast of the United States, with a large concentration of locations in the state of Oregon.
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Hand bunch of 12 pink roses wrapped in cellophane.
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5 Reviews
Sing a happy song with Phoolwala's elegant wish combo. The beautiful blooming roses along with a delicious black forest cake can be gifted in any joyous occasion.
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Yellow roses indicate friendship. Amaze your acquaintances with this pretty arrangement of yellow roses and let them know how special they are.
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PHW-14RR-Glass vase-NW
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Glass Vase arrangement of 10 pink roses and 24 pieces Ferrerorocher Chocolate
Orchids are the real trendsetter. Greet your buddies with the romantic orchids and allow them to enter your heart instantly.
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Pink Sweet
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subset: commoncrawl


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Not bad, bit light on the wheat taste, somewhat dry after taste. Gassed up beyond belief though & foams like a fire extinguisher when poured
Purchased From
318 William Street Melbourne, VIC
Category: Beer Garden, Bar, Pub
Tue, 11 Jun 2019 07:15:11 +0000
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Chrome Os To Support External Display Size Adjustment
You are able to shop for racks in regional home accessory stores or perhaps browse the web for finding several models of hanging wine holder. Needless to say, you can get some appealing deals on rack styles online. With a little patience and effort, you can find some websites that sell refurbished and second-hand wine storage racks for rock bottom prices. However , before buying used wine racks ensure the condition is good and the material is in decent shape. If you occur to decide on a small rack for saving a handful of bottles, setting it up wouldn't normally be an issue. However , designed for installing large sized carrier it will be ideal to seek companies of a veteran contractor. No matter what your requirement may be, we have a hanging wine rack offered in meet the same.
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Victoriajacksonshow - Chrome os to support external display size adjustment. Chrome os will soon support external display size adjustment options for people who have an external display connected to their chromebook the new setting, which is currently being worked on by. Chrome os to support external display size adjustment. Chrome os will soon support external display size adjustment options for people who have an external display connected to their chromebook the new setting, which is currently being worked on by the chrome os team, will be found in the settings menu under the display settings sub menu, and after users click on the separate tab which shows up if an external display is connected. Chrome os will soon support display scaling for external. In an upcoming update to chrome os, google will add an option to the operating system's display settings which will allow users to easily adjust the scale of the ui on external displays this. How to connect an external monitor to a chromebook. How to connect an external monitor to a chromebook chris hoffman @chrisbhoffman july 20, click the status area at the bottom right corner of the screen and select the connected external screen related: master chrome os with these chromebook keyboard shortcuts if the external display is positioned physically above the chromebook, drag. Chromebooks get better support for external displays. Improved support for external displays in chrome os more and more chrome os feature surface these days, and today we're glad to inform our readers that chromium evangelist at google fran�ois. Chromebook with 4k 10bits external display support, that. Looking to buy a new lightweight laptop and unfortunately one of my only "fancy" requirements is that it can send 4k h 265 hdr signal to an. Display size for external displays incoming for chrome os. Display size for external displays incoming for chrome os february 6, 2018 by robby payne 6 comments in general, chrome os is an operating system that just works and gets out of your way. Multiple external displays w pixel 2? : chromeos. Chrome os is google's linux based operating system built around the chrome web browser that can run android apps as a lightweight os designed primarily for web based and app based computing, it is fast, secure, and resilient to viruses and malware multiple external displays w pixel 2? as long as both of your external monitors support. Connect your chromebook to a monitor chromebook help. You can connect your chromebook to a monitor or tv with an hdmi, displayport, dvi, or vga port sometimes you need an adapter cable to do this to learn what type of cable you need, check the instructions included with your chromebook find the display output and input ports on your chromebook. Using an external monitor with your chromebook. To use chrome os on a larger screen than the one built into your notebook to optionally connect your chromebook to an external monitor, television, or projector, first connect the device to your chromebook using the appropriate cable see model specific instructions below.
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Towards the end of November 2017, A-Core of Idaho Concrete Pouring Division was hired to pour a shop slab in an existing structure at a large steel erection company in Idaho Falls, ID. The customer called A-Core for several reasons to tackle this project starting with the great relationship we have built throughout the years, competitive pricing and what sets us apart from the our competitors is our laser screed. The 12,000 square foot shop had a dirt floor that A-Core had to excavate down 6" all throughout, as well as excavate as needed for the footings required for the customer to install their cranes. From that point, the grade was leveled and compacted. We then tied rebar 18" on center throughout the slab as well as adding rebar as needed for the crane footings. Concrete was then pumped into the building where we were able to use our laser screed, making the slab perfectly flat. The finish of the slab required us to use our riding power trowel, giving the slab a nice slick finish. Our pouring division was able to complete the project start to finish in less than a week. A-Core then took the extra step to have the slab tested for its flatness where we were graded very high / very flat. Overall, the owner of the steel company called A-Core's team thanking us for completing the job on time, on budget and he said that the slab looked incredible.
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Nitric oxide binding at the mononuclear active site of reduced Pyrococcus furiosus superoxide reductase
Edited by Jack Halpern, University of Chicago, Chicago, IL, and approved January 31, 2003 (received for review November 11, 2002)
Nitric oxide (NO) has been used as a substrate analog to explore the structural and electronic determinants of enzymatic superoxide reduction at the mononuclear iron active site of Pyrococcus furiosus superoxide reductase (SOR) through the use of EPR, resonance Raman, Fourier transform IR, UV-visible absorption, and variable-temperature variable-field magnetic CD spectroscopies. The NO adduct of reduced SOR is shown to have a near-axial S = 3/2 ground state with E/D = 0.06 and D = 12 ± 2 cm−1 (where D and E are the axial and rhombic zero-field splitting parameters, respectively) and the UV-visible absorption and magnetic CD spectra are dominated by an out-of-plane NO−(π*)-to-Fe3+(dπ) charge–transfer transition, polarized along the zero-field splitting axis. Resonance Raman studies indicate that the NO adduct is six-coordinate with NO ligated in a bent conformation trans to the cysteinyl S, as evidenced by the identification of ν(N–O) at 1,721 cm−1, ν(Fe–NO) at 475 cm−1, and ν(Fe–S(Cys), at 291 cm−1, via 34S and 15NO isotope shifts. The electronic and vibrational properties of the S = 3/2 {FeNO}7 unit are rationalized in terms of a limiting formulation involving a high-spin (S = 5/2) Fe3+ center antiferromagnetically coupled to a (S = 1) NO− anion, with a highly covalent Fe3+−NO− interaction. The results support a catalytic mechanism for SOR, with the first step involving oxidative addition of superoxide to form a ferric-peroxo intermediate, and indicate the important roles that the Fe spin state and the trans cysteinate ligand play in effecting superoxide reduction and peroxide release.
Over the past 4 yr, evidence has accumulated for a novel pathway for detoxification of reactive oxygen species that is specific for anaerobic and microaerophilic microorganisms (1–3). The key enzyme in this pathway is superoxide reductase (SOR), which catalyzes the reduction of superoxide to hydrogen peroxide (4), with rubredoxin as the probable physiological electron donor (2, 5). Although all SORs have a β-barrel domain containing a unique type of mononuclear Fe center that serves as the site for superoxide reduction (6, 7), some have an additional N-terminal domain that contains an intrinsic rubredoxin-like mononuclear Fe site, which is ligated by four cysteines in a distorted tetrahedral arrangement analogous to that found in desulforedoxin (6). These two classes are conveniently referred to as 1Fe- and 2Fe-SORs, but they are also known by their trivial names, neelaredoxins and desulfoferrodoxins, respectively.
Spectroscopic and crystallographic studies of the 1Fe-SOR from Pyrococcus furiosus (7–9) and the 2Fe-SOR from Desulfovibrio desulfuricans (6, 10, 11) have shown that the mononuclear iron active site is ligated by four equatorial histidines (3ɛN and 1δN) and one axial cysteinate in a square-pyramidal arrangement. The sixth coordination site appears to be occupied by a monodentate glutamate in the oxidized state but is vacant or occupied by a weakly coordinated water molecule in the reduced state, thereby providing a site for superoxide binding and reduction. These structural studies, combined with recent mutagenesis and pulse radiolysis kinetic results (12–16), have led to the proposal for the catalytic mechanism shown in Fig. 1. The key steps involve oxidative addition of superoxide to the ferrous form of SOR to yield a ferric-peroxo intermediate, protonation possibly by a conserved lysine residue in the reduced active-site pocket to yield a ferric-hydroperoxo intermediate, and dissociation of the ferric-hydroperoxo intermediate, via Fe–O bond cleavage coupled with glutamate binding, to yield the H2O2 product. This mechanism is further supported by the recent characterization of a transient ferric-peroxo species in peroxide-treated samples of a variant of Desulfoarculus baarsii in which the active-site glutamate is replaced by alanine (17).
Characterization of enzymatic intermediates is required for both detailed understanding of the mechanism of SOR and addressing the key questions of how and why the SOR active site preferentially catalyzes reduction rather than dismutation of superoxide. However, these intermediates are short lived and difficult to study experimentally. Nitric oxide (NO) has been extensively used as a substrate analog of molecular oxygen to form stable nitrosyl derivatives that provide insight into oxygen transport and activation intermediates in many heme (18–21) and nonheme (22–29) iron enzymes. Hence, we report here the formation and spectroscopic characterization of a stable NO-bound derivative of the reduced 1Fe-SOR from P. furiosus using the combination of EPR, UV-visible absorption, and variable-temperature, variable-field magnetic CD (VTVH MCD), resonance Raman, and Fourier transform IR (FTIR) spectroscopies. The structural and electronic characterization of the NO adduct of SOR facilitates understanding of how the active site is tuned for oxidative addition of superoxide and release rather than intraligand cleavage of the peroxide product.
Materials and Methods
Biochemical Techniques and Sample Preparation.
Recombinant natural abundance and 34S globally enriched P. furiosus SOR was over-expressed in Escherichia coli and purified to homogeneity according to published procedures (8, 9). Unless otherwise indicated, the samples of P. furiosus SOR used in this work were in 100 mM Hepes buffer at pH 7.5 and were reduced by using 10 mM ascorbate. NO derivatives were prepared under strictly anaerobic conditions by adding an NO generator, methylamine hexamethylene methylamine (MAHMA) NONOate (Cayman Chemical, Ann Arbor, MI) or by exchanging the headspace above the SOR solution with NO gas. 14NO gas (>98%, Aldrich) and 15NO gas (99%, ICON Isotopes, Summit, NJ) were further purified before use by bubbling through a concentrated KOH solution to remove NO2. No changes in pH were detected on addition of MAHMA NONOate or exposure to NO gas. All samples were handled in a Vacuum Atmospheres (Hawthorne, CA) glove box (<1 ppm O2).
Spectroscopic Methods.
X-band (≈9.6 GHz) EPR spectra were recorded on a Bruker (Billerica, MA) ESP-300E EPR spectrometer with a dual-mode ER-4116 cavity and equipped with an Oxford ESR-9 flow cryostat (4.2–300 K). Spin quantitations were assessed as previously described (8), and EPR simulations were carried out by using the simfonia software package (Bruker). Resonance Raman spectra were recorded as described (9) on samples frozen at 17 K by using a scanning Instruments SA (Edison, NJ) Ramanor U1000 spectrometer fitted with a cooled RCA-31034 photomultiplier tube by using lines from a Coherent Sabre 100 10-W Argon Ion laser (Coherent Radiation, Palo Alto, CA). FTIR measurements were recorded by using a Bio-Rad FTS 575C spectrometer. Absorption spectra were recorded on Shimadzu UV301PC spectrophotometer. VTVH MCD measurements were recorded on samples containing 55% (vol/vol) glycerol by using a Jasco (Easton, MD) J-715 (180–1,000 nm) spectropolarimeter mated to an Oxford Instruments Spectromag 4000 (0–7 T) split-coil superconducting magnet. VTVH MCD saturation magnetization data of the SOR S = 3/2 iron-nitrosyl species were analyzed according to the published procedure (30), by using software supplied by Frank Neese and Edward I. Solomon (Stanford University, Stanford, CA).
No X-band EPR signals were observed for ascorbate-reduced samples of P. furiosus SOR, but intense resonances corresponding to two overlapping S = 3/2 species were observed in samples treated with NO generator, methylamine hexamethylene methylamine NONOate. For samples containing NO and SOR in an approximate 1:1 stoichiometry (Fig. 2), the major component is a rhombic resonance with g = 4.34, 3.76, 2.00 that is readily rationalized in terms of a conventional spin Hamiltonian as originating from the lower Ms = ±1/2 doublet of an S = 3/2 ground state with E/D = 0.06 and D > 0 parameters, where D and E are the axial and rhombic zero-field splitting parameters, respectively. The minor resonance exhibits a more axial resonance with g = 4.07, 4.00, 2.00 that originates from the lower Ms = ±1/2 doublet of an S = 3/2 ground state with E/D = 0.01 and D > 0. No resonance from the upper Ms = ±3/2 doublet was observed over the temperature range 4–60 K. Consequently, estimates of the separation between the Ms = ±1/2 and ±3/2 doublets (2D) were obtained by fitting plots of the EPR intensity vs. 1/T to a Boltzmann population distribution over a two-level system: D = 12 ± 2 cm−1 for the E/D = 0.06 component and D = 5 ± 1 cm−1 for the E/D = 0.01 component. Quantitation vs. a CuEDTA standard indicates that the entire resonance corresponds to 20% of the Fe containing SOR, and simulation of the spectra as the sum of two overlapping resonances revealed that the E/D = 0.06 and 0.01 species account for 84% and 16%, respectively. The substoichiometric spin quantitation is attributed to reversible binding of NO, because both resonances are progressively lost on repeated exchange of the headspace gas with Ar with continuous stirring. Moreover, redox cycling and exposure to up to a 3-fold excess of NO did not result in any significant loss of Fe from P. furiosus SOR, as judged by quantitative restoration of the oxidized absorption spectrum (8), after ascorbate reduction, NO treatment, and reoxidation with hexachloroiridate.
The origin of the heterogeneity in the ground-state properties of the NO adduct of reduced SOR was investigated by EPR studies as a function of pH, exposure to light, and the NO:SOR stoichiometry. The ratio of the E/D = 0.01 and 0.06 S = 3/2 species was not significantly perturbed by varying the pH over the range 5.5–9.0, and both resonances were lost at pH >9.5. In addition, neither resonance exhibited significant photolability, as evidenced by EPR studies at 10 K, while irradiating the sample in the cavity with a Xe arc lamp. However, the ratio of the intensities of the E/D = 0.01 and 0.06 S = 3/2 species was found to depend on the stoichiometry of NO to SOR. As the stoichiometry was increased from 0.3 to 3.0, the spin quantitation of the entire S = 3/2 resonance increased from 15% to 30% of the Fe-containing SOR, and the resonance changed from being almost exclusively that of the E/D = 0.06 species to being a 60:40 mixture of the E/D = 0.06 and 0.01 species.
Analogous near-axial S = 3/2 EPR signals to those observed for SOR have been observed for the nitrosyl adducts of a wide range of reduced mononuclear nonheme enzymes (22–27) and ferrous nitrosyl inorganic complexes (28, 31, 32). Under Enemark/Feltham notation (33), these species are conveniently represented as {FeNO}7, which treats the iron-nitrosyl as a bracketed unit with a superscript to represent the total number of Fe d and NO π* electrons. Detailed spectroscopic studies and electronic structure calculations for complexes containing S = 3/2 {FeNO}7 units (31, 32) have shown that the ground- and excited-state properties are best rationalized in terms of a limiting formulation involving high-spin Fe3+ (S = 5/2) antiferromagnetically coupled to NO− (S = 1). The EPR results for the nitrosyl adduct of ferrous SOR, therefore, support oxidative addition of NO to yield species with substantial Fe3+-NO− character.
Absorption and VTVH MCD.
The room temperature absorption and 4.2 K MCD spectra for the NO adduct of ascorbate-reduced P. furiosus SOR are shown in Fig. 3. The NO-treated samples were prepared by exposing samples containing 55% (vol/vol) glycerol to an atmosphere of NO for 30 sec before transfer under Ar into sealed cuvettes for the spectroscopic measurements. Parallel EPR studies on identical samples frozen at the same time as MCD samples exhibited EPR spectra very similar to those shown in Fig. 2, with the total S = 3/2 resonance accounting for 20% of the Fe containing SOR and 90% of this resonance arising from the E/D = 0.06 component.
Ascorbate-reduced SOR is colorless and has no significant absorption or MCD bands in the 14,000–29,000 cm−1 region. On addition of NO, the solution turns a red–brown color, and the absorption spectrum is dominated by a well-resolved band centered at 21,050 cm−1 (475 nm; ɛ = 530 M−1⋅cm−1) and a shoulder centered near 28,000 cm−1 (357 nm; ɛ ≈ 900 M−1⋅cm−1; see Fig. 3). Analogous absorption bands have been reported for the S = 3/2 NO adducts of a wide range of nonheme proteins and inorganic complexes (22, 28, 31, 34, 35) and have been attributed to charge transfer (CT) transitions associated with the{FeNO}7 unit. The 4.2 K MCD spectrum of the NO adduct of ascorbate-reduced P. furiosus SOR in the 14,000 – 29,000 cm−1 region correlates closely with the absorption spectrum and is dominated by a positive MCD C term centered at 21,050 cm−1, with less pronounced positive C terms apparent at 28,000 cm−1 (357 cm−1) and as a shoulder at ≈23,500 cm−1 (425 nm; see Fig. 3). The negative C term centered at 12,400 cm−1 that is present in the samples before and after NO treatment corresponds to the 5T2g (dxy) → 5Eg (dx2−y2) ligand field transition of the square-pyramidal high-spin Fe2+ center in unreacted reduced SOR. Evidence for unreacted reduced SOR is also apparent by the characteristic pattern of (Cys)S−-to-Fe2+ CT bands (8) that are observed in the low-temperature MCD spectrum in the 29,000–40,000 cm−1 region (data not shown). In agreement with EPR spin quantitations, which indicated that only 20% of the reduced SOR is in the NO-bound form, the intensity of (Cys)S−-to-Fe2+ CT MCD bands in the NO-treated sample was ≈80% of that observed for samples before NO treatment.
Well-resolved absorption bands centered between 20,000 and 24,000 cm−1 that give rise to positive MCD C-terms centered at the same energies are a unifying attribute of the absorption and MCD spectra of all S = 3/2 {FeNO}7 species investigated thus far (28, 31, 34). This transition has been assigned to the out-of-plane NO−(π*)-to-Fe3+(dπ) CT within the idealized Fe3+-NO− unit, because these orbitals are predicted to have optimal overlap based on SCF-Xα-SW calculations (31). To test the validity of the proposed assignment, the transition polarization was assessed via VTVH MCD saturation magnetization studies on the MCD band centered at 21,050 cm−1 (475 nm) (see Fig. 7, which is published as supporting information on the PNAS web site, www.pnas.org). The results indicate a uniaxial transition polarized along the unique (z) axis of the predominantly axial zero-field splitting. This is in complete accord with assignment to an out-of-plane NO−(π*)-to-Fe3+(dπ) CT transition, and the MCD magnetization data indicate that the Fe–NO bond is collinear with the zero-field splitting axis.
Resonance Raman and FTIR.
To assign vibrational bands based on 15NO isotope shifts, samples for resonance Raman and FTIR studies were prepared by incubating concentrated samples of ascorbate-reduced SOR, 4–5 mM, under an atmosphere of 14NO or 15NO gas. Parallel EPR studies of the samples used for resonance Raman and FTIR investigations showed resonances that were almost exclusively (>95%) from the S = 3/2 species with E/D = 0.06.
In accord with the assignment of the absorption band at 21,050 cm−1 (475 nm) to the out-of-plane NO−(π*)-to-Fe3+(dπ) CT transition, resonance Raman studies using 476-nm excitation revealed enhancement of vibrational modes associated with the {FeNO}7 unit (see Fig. 4). The high-frequency intraligand stretching region shows a band that shifts from 1,721 cm−1 in the 14NO adduct to a shoulder at 1,690 cm−1 in the 15NO adduct, in addition to modes at 1,552, 1,616, and 1,668 cm−1 that show no 15NO/14NO shift and are assigned to vibrations of the polypeptide backbone (9). On the basis of the 31-cm−1 isotope shift, the 1,721 cm−1 band is assigned to the ν(N–O) stretching mode, which is predicted to exhibit a 31-cm−1 14N/15N isotope shift based on a simple diatomic oscillator approximation. A band with a 32-cm−1 15NO/14NO shift was also observed in the FTIR spectrum at 1,728 cm−1 (see Fig. 8, which is published as supporting information on the PNAS web site). The difference in the frequencies of the ν(N–O) stretching mode as determined by resonance Raman (1,721 cm−1) and FTIR (1,728 cm−1) is attributed to the measurement conditions, i.e., frozen solution at 17 K for Raman and aqueous solution at room temperature for FTIR.
The low-frequency metal-ligand stretching region shows one 15NO/14NO-sensitive vibration that shifts from 475 cm−1 in the 14NO adduct to 468 cm−1 in the 15NO adduct (Fig. 4). Both ν(Fe–NO) stretching and δ(Fe–N–O) bending modes are expected in this region, and these modes are likely to be extensively mixed. Nevertheless, several lines of evidence favor assignment of the band at 475 cm−1 to a mode that predominantly involves ν(Fe–NO) stretching. First, in the absence of a specific enhancement mechanism, bending modes generally exhibit weaker resonance enhancement than stretching modes and hence are weaker in resonance Raman spectra. This general observation is borne out by resonance Raman studies of nitrosyl hemes in which the ν(Fe–NO) stretching and δ(Fe–N–O) bending modes have been rigorously assigned based on 15NO, N18O, and 15N18O isotope shifts and normal mode calculations (19–21). The ν(Fe–NO) stretching modes are invariably more strongly enhanced than the δ(Fe–N–O) bending modes, and the enhancement of the bending mode generally decreases as the Fe–N–O angle approaches 180°. Second, the observed 15N downshift, 7 cm−1, is consistent with a bent FeNO unit with an angle closer to 180° than to 90°. A ν(Fe–NO) stretching mode at 475 cm−1 is predicted to have a 15N downshift in the range 5–13 cm−1 based on a simple two-body diatomic oscillator approximation, with the smallest shift predicted for Fe–N–O bond angles close to 180°, and the largest shift predicted for Fe–N–O bond angles close to 90°. The range of 15N downshifts for ν(Fe–NO) stretching modes predicted for this simple model is generally in good agreement with experimental data obtained for well characterized nitrosyl hemes, i.e., downshifts as low as 2 cm−1 for linear FeNO and as high as 14 cm−1 for bent FeNO with an Fe–N–O angle of 115° (19–21).
In addition to the ν(Fe–NO) and ν(N–O) stretching modes, vibrational modes associated with the Fe-S(Cys) unit are also weakly enhanced in resonance with absorption band at 21,050 cm−1 (475 nm). A comparison of the resonance Raman spectra obtained for the NO adducts of natural abundance and 34S globally labeled SOR by using 476-nm excitation revealed two 34S-sensitive bands, located at 291 cm−1 and 758 cm−1, that exhibit 3-cm−1 downshifts in the 34S-labeled samples (see Fig. 5). These two bands are readily assigned to the ν(Fe–S) and ν(S–C) stretching modes of the Fe–S(Cys) unit, respectively, on the basis of previous assignments for oxidized P. furiosus SOR (9). Enhancement of vibrations associated with the (Cys)S–Fe–NO unit was observed with 476-nm excitation, but not with 647-nm excitation [the optimal wavelength for enhancing vibrations of the Fe–S(Cys) unit in oxidized P. furiosus SOR (9)] (see Fig. 5). Hence the observed vibrational modes associated with the Fe–S(Cys) unit are not the result of partial oxidation. Rather, they are enhanced via kinematic coupling with the ν(Fe–NO) stretching mode and/or an excited-state A-term mechanism involving the competing π interactions within the trans (Cys)S–Fe–NO unit. Irrespective of the enhancement mechanism, the observation of vibrational modes associated with the Fe–S(Cys) unit demonstrates that cysteinate is ligated trans to NO in the NO adduct of SOR that is responsible for the S = 3/2, E/D = 0.06 species.
Interaction of ascorbate-reduced P. furiosus SOR with NO has been shown to result in the reversible formation of a stable six-coordinate derivative of the mononuclear Fe active site with NO bound trans to the cysteinate ligand. The ground- and excited-state electronic properties of this NO adduct, i.e., near-axial S = 3/2 ground-state with zero-field splitting parameters E/D = 0.06 and D = 12 ± 2 cm−1 and visible absorption and low-temperature MCD spectra dominated by a well-resolved band centered at 21,050 cm−1 (475 nm), are characteristic of nonheme iron proteins and inorganic complexes containing S = 3/2 {FeNO}7 units (22, 31, 34). Moreover, on the basis of the detailed spectroscopic and electronic structure calculations that are available for inorganic complexes containing S = 3/2 {FeNO}7 units (31, 32), the ground- and excited-state properties are best rationalized in terms of a limiting formulation involving a high-spin (S = 5/2) Fe3+ center antiferromagnetically coupled to a (S = 1) NO− anion. The resulting Fe3+–NO− interaction is highly covalent as a result of strong NO− σ- and π-donor bonding to Fe3+, and the strong π overlap is manifest by the visible absorption band at 21,050 cm−1, which is attributed to the out-of-plane NO−(π*)-to-Fe3+(dπ) CT transition that is shown to be polarized along the unique (z) axis of the predominantly axial zero-field splitting via VTVH MCD studies.
The resonance Raman and FTIR studies of the NO adduct of reduced SOR reported herein constitute the first vibrational characterization, to our knowledge, of a S = 3/2 {FeNO}7 unit in a mononuclear nonheme iron enzyme and provide assessment of the structure and bonding within the trans (Cys)S–Fe–NO unit. Using excitation at 476 nm into the out-of-plane NO−(π*)-to-Fe3+(dπ) CT transition, resonance Raman studies have identified the ν(N–O) stretching mode at 1,721 cm−1 and ν(Fe–NO) stretching mode at 475 cm−1, on the basis of 15NO downshifts of 31 and 7 cm−1, respectively. In accord with the limiting Fe3+–NO− formulation, the frequency of the intraligand ν(N–O) stretching mode is substantially reduced compared with NO gas, ν(N–O) at 1,876 cm−1 (36), as a result of electron transfer into the NO π* orbital. The only other vibrational data for a biological {FeNO}7 unit come from resonance Raman studies of the NO adduct of deoxyhemerythrin by using 647-nm excitation. Although the ν(N–O) stretching mode was not observed, a band at 433 cm−1 and a weak shoulder at 421 cm−1 were assigned to the ν(Fe–NO) and δ(Fe–N–O) modes, respectively, of the {FeNO}7 unit, based on 6–7 cm−1 15NO and N18O downshifts (29). The frequencies of the ν(Fe–NO) modes dictate a substantially weaker Fe–NO bond in hemerythrin than in SOR, and this is likely to be a consequence of a strong H-bonding interaction between the bent FeNO and the μ-hydroxo bridge of the diiron center (29).
Greater insight into the structure of the {FeNO}7 unit in the NO adduct of SOR is provided by comparison with the resonance Raman data for the S = 3/2 {FeNO}7 unit in the inorganic complexes, Fe(L)(NO)(N3)2 (L is N,N′,N′′-trimethyl-1,4,7-triazacyclonane) and Fe(EDTA)(NO), which have Fe–N–O bond angles of 156° (31, 37). Both complexes exhibit resonance Raman spectra similar to that of the NO adduct of SOR with bands at 1,712 and 1,776 cm−1, respectively, that were identified as ν(N–O) stretching modes based on 15NO downshifts of 31–32 cm−1, and strong bands at 497 and 496 cm−1, respectively, with downshifts of 6–8 cm−1 (31). However, the bands at 497 and 496 cm−1 were assigned to δ(Fe–N–O) bending rather ν(Fe–NO) stretching (31) on the basis of IR studies of metal nitrosyl complexes, which indicated larger 15NO isotope shifts for δ(M–N–O) modes (6–15 cm−1) than for ν(M–NO) modes (1–6 cm−1) (38, 39). Subsequent resonance Raman studies of nitrosyl hemes (19–21) have clearly shown that these ranges are applicable only to near-linear MNO units. Moreover, the pattern of isotope shifts observed for the 497 and 496 cm−1 bands in these complexes, i.e., larger isotope shift for 15NO than N18O (31), is a characteristic of the ν(M–NO) modes of bent FeNO units in nitrosyl hemes (20). Taken together with the strong resonance enhancement of these bands, reassignment to modes predominantly involving ν(Fe–NO) stretching is clearly warranted.
The structure of the FeNO unit in the six-coordinate nitrosyl adduct of SOR is likely to be very similar to that found in the structurally characterized six-coordinate Fe(L)(NO)(N3)2 complex (Fe–N–O angle = 156°), on the basis of similar frequencies for the ν(N–O) and ν(Fe–NO) modes. The most significant difference is a weaker Fe–NO bond in SOR, as evidenced by the 21-cm−1 decrease in the frequency of the ν(Fe–NO) mode. This is attributed to the mutual trans influence of the cysteinate and NO− ligands, which compete for the same set of Fe d-orbitals for both σ- and π-bonding interactions (see Fig. 6). The principal bonding interactions within the {FeNO}7 involve π-donor interactions involving the half-filled π* orbitals on NO− and the half-filled Fe3+ dxz and dyz orbitals and the σ-donor interaction between the filled σ* orbital on NO− and the half-field Fe3+ dz2 orbital (31). For the Fe-S(Cys) fragment, the principal bonding interactions involve π-donor interactions involving the filled S pπ and ppseudo σ orbitals and the half-filled Fe3+ dxz and dyz orbitals and the σ-donor interaction between the filled S ppseudo σ orbital and the half-field Fe3+ dz2 orbital (8). Evidence for the weakening of the Fe–S(Cys) bond in the NO adducts of SOR relative to the six-coordinate high-spin Fe3+ site in the oxidized enzyme comes from the 32-cm−1 decrease in the frequency of the vibrational mode that primarily involves Fe-S(Cys) stretching [323 cm−1 in oxidized native SOR (9) compare with 291 cm−1 in the NO adducts of SOR]. The trans influence of a cysteinate ligand on the Fe–NO bonding interaction is also evident in the resonance Raman studies of six-coordinate nitrosyl hemes containing S = 1/2 {FeNO}7 units. Nitrosyl heme proteins with cysteinate trans to the bound NO exhibit ν(Fe–NO) frequencies 10–20 cm−1 lower than those with histidyl ligation.
Thus far, it has not been possible to characterize the optical and vibrational properties of the S = 3/2 {FeNO}7 species with E/D = 0.01 that is progressively formed as the NO-to-SOR stoichiometry increases. Consequently, the origin of the heterogeneity in the NO-bound forms of SOR that is apparent in EPR studies is unclear at present. Mutagenesis experiments involving the glutamate and lysine residues that are in close proximity to the substrate-binding site are currently in progress to assess whether the observed heterogeneity is a consequence of differences in hydrogen-bonding interactions. An alternative possibility is that the more axial E/D = 0.01 species corresponds to a five-coordinate {FeNO}7 species in which the Fe-S(Cys) bond has been cleaved. Similar near-axial S = 3/2 {FeNO}7 EPR signals have been observed in several nonheme Fe proteins before binding substrate or substrate analogs to form six-coordinate S = 3/2 {FeNO}7 species, which exhibit more rhombic resonances similar to the E/D = 0.06 species observed in this work (22, 27). In addition, the trans influence of NO binding is responsible for cleavage of weak proximal Fe–His bonds in many ferrous heme proteins, particularly those with regulatory roles involving the sensing of small molecules such as NO (soluble guanylate cyclase), O2 (FixL), and CO (CooA) (40). Reversible NO-induced cleavage of the Fe–S(Cys) bond in SOR, coupled with reversible nitrosylation of the free thiolate, could therefore be invoked to explain the dependence of the heterogeneity on the NO concentration.
Comparison of the ν(N–O) and ν(Fe–NO) frequencies for the six-coordinate S = 3/2 {FeNO}7 species in the NO adduct of SOR and the Fe(L)(NO)(N3)2 complex with those of six-coordinate S = 1/2 in heme proteins reveals dramatic differences in the bonding in S = 1/2 and 3/2 {FeNO}7 species. Six-coordinate S = 1/2 {FeNO}7 species in heme proteins have much stronger Fe–NO bonds, as evidenced by ν(Fe–NO) frequencies in the range 536–558 cm−1 (20, 21, 41), and much weaker N–O bonds, as evidenced by ν(N–O) frequencies in the range 1,555–1,624 cm−1 (20, 21). Although no clear consensus has emerged concerning the most appropriate description of the electronic structure and bonding in S = 1/2 {FeNO}7 species (18, 32, 42), the increase in Fe–NO bond strength and concomitant decrease in the N–O bond strength, compared with S = 3/2 {FeNO}7 species, appear to be a direct consequence of increased σ-donation into the empty dz2 orbital that results from lowering the Fe spin state from high to low or intermediate spin.
Finally, we address the implications of the spectroscopic characterization of the NO adduct of SOR for understanding how the mononuclear Fe active site of SOR is tuned for superoxide reduction. Clearly, the formation of the NO adducts of reduced SOR by oxidative addition of NO at the vacant coordination site of the ferrous active site is consistent with an inner-sphere mechanism for superoxide reduction, with the first step involving oxidative addition of superoxide to yield a ferric-peroxo intermediate. Moreover, the oxidative addition of π-bonded diatomics is enhanced by the electron-donating ability of the trans cysteinate ligand. Absorption and VTVH MCD studies of the square-pyramidal ferrous active site have shown intense (Cys)S−-to-Fe2+ CT bands (8), indicative of strong pπ-dπ S–Fe bonding. The resulting increased electron density in the Fe dπ orbitals therefore facilitates ligand reduction via Fe dπ to ligand π* electron transfer. The S = 3/2 {FeNO}7 species in SOR is proposed as a stable analog of the S = 5/2 {FeOO}9 high-spin ferric (hydro)peroxo intermediate, albeit with one rather than two electrons in each of the π* orbitals (see Fig. 6). Filled π* orbitals, coupled with the trans influence of the cysteinate, would be expected to weaken the Fe–OO(H) bond relative to the Fe–NO bond as a result of decreased π*–dπ bonding. This accounts for the instability of the ferric (hydro)peroxo intermediate with respect to cleavage of the Fe–OO(H) bond. On the basis of the differences in the bonding that are apparent from the vibrational studies of S = 1/2 and S = 3/2 {FeNO}7, a high-spin ferric (hydro)peroxo intermediate is likely to be essential to promote breakdown via Fe–O rather O–O bond cleavage. This is in accord with recent studies by the Solomon and Que groups, which have shown that high-spin Fe3+-(alkyl)peroxo have much weaker Fe–O bonds and much stronger O–O bonds than their low-spin counterparts (43, 44). Overall, characterization of the NO adducts of SOR indicates that the Fe spin state and the trans cysteinate ligand play important roles in effecting superoxide reduction and peroxide release at the SOR active site. By providing a stable analog of the ferric (hydro)peroxo intermediate, the NO adduct of SOR is likely to be very useful for probing H-bonding interactions in the active-site pocket.
This work was supported by a grant from the National Institutes of Health (GM60326 to M.W.W.A. and M.K.J.) and a National Science Foundation Research Training Group Award (DBI9413236) to the Center for Metalloenzyme Studies.
↵¶ To whom correspondence should be addressed. E-mail: johnson{at}chem.uga.edu.
This paper was submitted directly (Track II) to the PNAS office.
- superoxide reductase;
- variable-temperature variable-field magnetic CD;
- charge transfer;
- Fourier transform IR
- Received November 11, 2002.
- Copyright © 2003, The National Academy of Sciences
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Understanding Jessner Peel
Delivering a broad spectrum of benefits, the Jessner Peel dries out active acne, reduces acne scarring, smoothens out fine lines and wrinkles, and lightens skin discoloration due to hyperpigmentation. It is also effective for stimulating collagen, refining open pores and rejuvenating sun-damaged skin.
It can be used on non-facial areas as well, making it an effective treatment for acne on the back, chest or arms and for the treatment of in-grown hair.
A combination of three chemicals, lactic acid, salicylic acid and resorcinol, the Jessner Peel is stronger and more aggressive than most superficial peels. It is a medium depth peel, which means it penetrates through the epidermis but not into the dermis. This makes it ideal as a 'pre-treatment peel' prior to even deeper and more aggressive treatments.
Lactic acid assists in exfoliation of the skin, Salicylic acid in penetration of the ingredients and Resorcinol in the treatment of acne.
Generally, around 2-5 coats of the peel are applied, followed by a calming mask after the session.
The peel can be repeated at 4 week intervals until the desired effect is achieved.
A warm, tingling sensation may be experienced at the time the peel is applied. The skin may then look white and frosted – for a few hours only.
Over the next few days, the skin will appear progressively more inflamed – going from red in colour to brown. This is because the peeling process is underway.(deleted the phrase about inflamed skin as it feels like a repetition from the opening of the para)
The skin will also feel dry and uncomfortable. But once it has peeled way, a glowing complexion will be revealed.
Since the peel penetrates deeper with each coat of solution applied, recovery time increases accordingly as well.
- Do not opt for this peel if allergic to milk, aspirin or onion extract
- Avoid if skin conditions like eczema, psoriasis or dermatitis are present
- Avoid using Retinoids from 5 days prior to the peel
- Avoid opting for this peel if pregnant or lactating
- Avoid laser treatments, waxing or depilatory creams for 2 weeks prior to the treatment.
- Do not apply anything on the face for the first hour
- After 1 hour apply the recommended skin lubricant and use it every 2 hours to keep the skin moisturized
- For the first 2 days do not wet the face with hot water, splash cold water if any discomfort
- For the first 4 days avoid heat or excessive sweating
- Within a week the peeling process will be done. Avoid applying any makeup till then.
- Avoid laser treatments, waxing or depilatory creams for 2 weeks after the treatment.
- For a minimum of a month, apply SPF50 sunscreen regularly.
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