Electron Transfer in Extremely Halophilic Bacteria
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Marcia Steinberg', 'PO_EMAI': None, 'PO_PHON': None}
Environmental stress in the form of high ionic strength                    has been surmounted by a number of organisms in a number of                     ways.  In general, little is known about electron transfer or                   coupled energy conservation in any of the extreme halophiles.                   In preliminary studies, the investigator has found that                         electron transfer mechanisms observed with proteins from                        nonhalophilic bacteria must be distinct from the extreme                        halophiles, as electrostatics appear to play an important role                  in the elctron transfer proecss.  Thus, proteins operating in                   the periplasmic space in moderate and extreme halophiles must                   control specificity by the use of factors other than                            electrostatics.  In addition, extreme and moderate halophiles                   appear to have redox proteins which have generally lower redox                  potentials, are strongly acidic, and in at least two cases have                 redox potentials which are ionic strength-dependent at high                     ionic strengths.  Thus it appears that in the course of                         adaptation to a high ionic strength environment, structural                     alterations at the molecular level have taken place.  It should                 be emphasized that halotolerant bacteria, those able to live                    both with and without salt, are not obviously different from                    fresh-water bacteria.  Three halophilic organisms will be                       studied with this grant.                                                             Soluble redox proteins (c-type cytochromes and iron-sulfur                 proteins) from these bacteria will be characterized in terms of                 location  and the effect of osmoregulators and ionic strength                   on redox potentials, spectral properties, and thermal                           denaturation.  Data will be analyzed in terms of known                          structural properties and supplemented by computer modeling                     utilizing 3-D structures of related proteins.  Finally, some                    basic physiological processes will be studied.   It is                          anticipated that the proposed studies will provide new                          insights into the molecular properties controlling biological                   electron transfer, a better understanding of the physiology of                  halophiles, and an increase in our knowledge of the structural                  and chemical parameters that control protein stability.
{'FirstName': 'Terrance', 'LastName': 'Meyer', 'PI_MID_INIT': 'E', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Terrance E Meyer', 'EmailAddress': 'temeyer@u.arizona.edu', 'NSF_ID': '000470813', 'StartDate': '04/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Arizona', 'CityName': 'TUCSON', 'ZipCode': '85721', 'PhoneNumber': '5206266000', 'StreetAddress': '845 N PARK AVE RM 538', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Arizona', 'StateCode': 'AZ', 'CONGRESSDISTRICT': '07', 'CONGRESS_DISTRICT_ORG': 'AZ07', 'ORG_UEI_NUM': 'ED44Y3W6P7B9', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF ARIZONA', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8718678.xml'}