The Novel Iron-Sulfur Clusters of Hydrogenase
{'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}
The objectives of this proposal are to expand our knowledge                     of the structure, function and chemical reactivity of                           biological iron-sulfur clusters, the most ubiquitous electron                   carriers in nature.  It has been shown that two hydrogenases                    from the anaerobic bacterium, Clostridium pasteurianum,                         contain a new type of iron-sulfur center, a 6Fe cluster,                        which is unprecedented in biological systems.  Moreover, it                     is intimately involved in catalyzing a chemical reaction, the                   activation of the simplest molecule, H2, and it covalently                      binds CO, a potent inhibitor.  One of the hydrogenases                          catalyzes a reversible reaction while the other                                 preferentially catalyzes H2 oxidation and mechanisms have                       been proposed to account for these differences.  In the                         period of this research the reactive 6Fe clusters will be                       modified with site-directed chemical probes, i.e. NO, N2O,                      PH3, CH3NC and O2, and modify the hydrogenase proteins  using                   amino-acid specific reagents.  The modified enzymes will be                     characterized by changes in the catalytic activities and by                     electron paramagnetic resonance spectroscopy (using                             isotopically-enriched enzymes and chemical probes), redox                       potentionmetry and peptide mapping.  This study will provide                    information on the structure of their novel 6Fe-clusters and                    the synergistic role of the cluster and the hydrogenase                         protein in H2 catalysis.                                                                                                                                        Proteins containing clusters of non-heme iron and inorganic                     sulfur are the most ubiquitous electron carriers in nature.                     The provide the cornerstone for such biological processes as                    respiration, photosynthesis and nitrogen fix ation and                          participate in innumerable metabolic processes.  A very                         recent development is the realization that iron-sulfur                          clusters fulfill functions other than or in addition to                         electron transfer.  This study focuses on an example of this.                   The two hydrogenases of Clostridium pasteurianum contain a                      novel iron-sulfur cluster that is involved in both electron                     transfer and catalysis and it covalently binds the inhibitor.                                                                                                   An elucidation of their catalytic mechanism is therefore of                     fundamental importance.  Dr. Adams has the expertise needed                     to pursue this project.
{'FirstName': 'Michael', 'LastName': 'Adams', 'PI_MID_INIT': 'W', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Michael W Adams', 'EmailAddress': 'adams@bmb.uga.edu', 'NSF_ID': '000290724', 'StartDate': '11/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Georgia Research Foundation Inc', 'CityName': 'ATHENS', 'ZipCode': '306021589', 'PhoneNumber': '7065425939', 'StreetAddress': '310 E CAMPUS RD RM 409', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Georgia', 'StateCode': 'GA', 'CONGRESSDISTRICT': '10', 'CONGRESS_DISTRICT_ORG': 'GA10', 'ORG_UEI_NUM': 'NMJHD63STRC5', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF GEORGIA RESEARCH FOUNDATION, INC.', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
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