Molecular Biology and Biochemistry of Nickel-Containing     Hydrogenases
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Eve Ida Barak', 'PO_EMAI': None, 'PO_PHON': None}
The hydrogenases of anaerobic organisms are fascinating                         metalloenzyumes that incorporate unusual and unexpected                         coenzymes to catalyze unusual oxidations and reductions.                        Three types of hydrogenases have been characterized to date                     from sulfate reducing bacteria:  the first from Desulfovibrio                   gigas contains non heme iron and redox active nickel (NiFe);                    the second from D. vulgaris contains exclusively non-heme                       iron (Fe) and the third purified from D. baculaturs contains                    non heme iron plus equivalent amounts of nickel and selenium                    (NiFeSe).  The immediate objectives are to develop the basic                    enzymological, biochemical and stuctural information required                   to understand the biological function of nickel and the roles                   of sulfur and silenmia in nickel catalysis.  Specific aims                      are  1) to purify and characterize the (NiFeSe) hydrogenase;                    2) To evaluate the potential of Se as a probe of the                            catalytic significance of nickel; 3) to study the activation                    of the (NiFe) hydrogenase; 4) to probe the catalytic redox                      cycling of the (NiFe) hydrogenase; 5) to determine the DNA                      sequences of the hydrogenase genes; 6) to study the                             mechanisms involved in cellular localization of the (NiFeSe)                    hydrogenases; and  7) to determine by site specific                             mutagenesis the amino acid residues responsible for the                         liganding of the four redox centers of the (NiFe)                               hydrogenases.
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{'Name': 'University of Georgia', 'CityName': 'ATHENS', 'ZipCode': '306020001', 'PhoneNumber': '7065425939', 'StreetAddress': '623 BOYD GRADUATE RESEARCH CTR', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Georgia', 'StateCode': 'GA', 'CONGRESSDISTRICT': '10', 'CONGRESS_DISTRICT_ORG': 'GA10', 'ORG_UEI_NUM': 'Q2LKTLYJM4P8', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF GEORGIA', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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