Assembly and Function of the Cofactors of Fumarate Reductasefrom Escherichia Coli
{'Code': '08070400', 'Directorate': {'LongName': 'Direct For Biological Sciences'}, 'Division': {'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Marcia Steinberg'}
The research proposed is intended to expand knowledge on how                    iron-sulfer clusters and covalent flavins assemble and                          function in membrane-bound protein complexes required for                       electron transport and energy conservation.  The studies are                    aimed at answering the existing questions relating to the                       interrelationship between the three iron-sulfur clusters                        known to be present in fumarate reductase and whether there                     is a requirement for a "flavin-ligating" enzyme to catalyze                     the formation of covalent flavin protein complexes.  The                        research will also address questions about the relationship                     between iron-sulfur cluster structure and protein sequence                      and the role of the individual clusters in electron                             transport.  Approaches used to meet these goals include                         genetic modification of fumarate reductase by both                              oligonucleotide-directed and chemical mutagenesis methods.                      The modified proteins will then be analyzed by biochemical                      assays in order to define the catalytic activity of the                         modified enzyme and its cellular location (membrane-bound or                    cytoplasmic).  In addition we will use biophysical                              approaches such as EPR and magnetic circular dichroism to                       monitor the function and structure of the iron-sulfur                           clusters of the enzyme.  This research will contribute to our                   understanding of how complex flavoprotein oxidoreductases                       assemble into functional protein complexes and thus help                        elucidate the path of electron transport through such                           proteins.
{'FirstName': 'Gary', 'LastName': 'Cecchini', 'EmailAddress': 'ceccini@itsa.ucsf.edu', 'StartDate': '04/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-San Francisco', 'CityName': 'San Francisco', 'ZipCode': '941034249', 'PhoneNumber': '4154762977', 'StreetAddress': '1855 Folsom St Ste 425', 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA'}
{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8715560.xml'}