US-Federal Republic of Germany Cooperative Research:  Low   Frequency ESR Studies of Cu-Cu Interactions
{'Code': '01090000', 'Directorate': {'Abbreviation': 'O/D', 'LongName': 'Office Of The Director'}, 'Division': {'Abbreviation': 'OISE', 'LongName': 'Office Of Internatl Science &Engineering'}}
{'SignBlockName': 'Christine French', 'PO_EMAI': None, 'PO_PHON': None}
This proposal for research on "Low Frequency ESR Studies of Cu-Cu               Interactions" between Dr. William E. Antholine of the Medical                   College of Wisconsin and Dr. Peter M. H. Kroneck of the Universitaet            Konstanz, FRG, is sponsored by NSF under the U.S.-Federal Republic              of Germany Cooperative Research Program.                                                                                                                        This research will attempt to demonstrate the efficiency of low-                frequency (S-band) electron spin resonance (ESR) for unravelling                the ESR spectra from ESR detectable binuclear copper sites. The                 researchers will compare ESR data from Cu(1.5)Cu(1.5) sites in N2OR             (nitrous oxide reductase)to ESR data from cytochrome oxidase, to                determine whether the Cu/a site is a mixed valence binuclear copper             site.  Analysis of line widths and strain parameters through                    spectral simulation is expected to account for the shape of these               ESR signals.  A demonstration of the enhanced sensitivity of the                half field lines at S-band for Cu(II)Cu(II) dimers in nitric oxide              treated tyrosinase, ceruloplasim, and nitrous oxide reductase will              be a useful result, by itself, for copper dimers.  The ESR group in             Wisconsin has pioneered the use of multifrequency ESR as a prime                spectroscopic modality for analysis of Cu(II) sites in biological               systems.  The group in Konstanz has studied the relationship                    between structure and function of catalytic centers in multicopper              proteins such as ascorbate oxidase and nitrous ovide reductase.                 Thus, the two groups will complement each other in carrying out the             long term goal of the project:  to develop techniques to extract                physical chemical data from cupric complexes in cells and eventually            in animal systems.
{'FirstName': 'William', 'LastName': 'Antholine', 'PI_MID_INIT': 'E', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'William E Antholine', 'EmailAddress': 'watholi@mcw.edu', 'NSF_ID': '000332827', 'StartDate': '09/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Medical College of Wisconsin', 'CityName': 'MILWAUKEE', 'ZipCode': '532263548', 'PhoneNumber': '4149558563', 'StreetAddress': '8701 WATERTOWN PLANK RD', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Wisconsin', 'StateCode': 'WI', 'CONGRESSDISTRICT': '04', 'CONGRESS_DISTRICT_ORG': 'WI04', 'ORG_UEI_NUM': 'E8VWJXMMUQ67', 'ORG_LGL_BUS_NAME': 'THE MEDICAL COLLEGE OF WISCONSIN, INC.', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '5936', 'Text': 'GERMANY (F.R.G.)'}
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