Collaborative Research:  Chemical and Genetic Modification  of Biological Iron-Sulfur Clusters:  Azotobacter Vinelandii Fereedoxin I
{'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}
Iron sulfur (Fe-S) proteins contain clusters composed                           predominately of Fe, S2- and cysteine residues.  These                          proteins are ubiquitous occuring in all known organisms and                     are central to every essential biological process.  Three                       types of clusters containing respectively, 1, 2, and 4 Fe                       atoms are now well characterized and recently clusters                          containg three Fe atoms have been discovered.  The first                        three exhibit multiple oxidation levels.  It has recently                       been shown that electron transport is not the sole function                     of these proteins.  It is now abundantly clear that the                         variety of Fe-S cluster structures is greater than previously                   recognized and continues to expand.  The chemistry is far                       more extensive than simple, reversible one-electron redox                       behavior.  The goal of this proposal is to ascertain how the                    primary sequence determines which type of cluster is                            functional in a given protein.  To achieve this goal the                        structures and reactivities of protein-bound 3 FE and 4 FE                      (Fe-S) clusters in A. vinelandii fereedoxin I (AVFD) will be                    studied in depth.  This small protein is ideally suited for                     such an investigation, as it expresses multiple forms and X-                    ray data is becoming available.  Consequently, it is planned                    to purify and crystallize the three new forms of AvFdI,                         characterize them physico-chemically, modify them by site                       directed mutagenesis, and purify and characterize the                           resulting fereedoxins.  This work may prove crucial to our                      quest to understand nitrogenase and other multicentered redox                   proteins containing Fe-S centers.  Support is strongly                          recommended with a high priority.
{'FirstName': 'Barbara', 'LastName': 'Burgess', 'PI_MID_INIT': 'K', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Barbara K Burgess', 'EmailAddress': 'bburgess@uci.edu', 'NSF_ID': '000273281', 'StartDate': '10/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-Irvine', 'CityName': 'IRVINE', 'ZipCode': '926970001', 'PhoneNumber': '9498247295', 'StreetAddress': '160 ALDRICH HALL', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '47', 'CONGRESS_DISTRICT_ORG': 'CA47', 'ORG_UEI_NUM': 'MJC5FCYQTPE6', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF CALIFORNIA IRVINE', 'ORG_PRNT_UEI_NUM': 'MJC5FCYQTPE6'}
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