Electron Transfer in the Cytochrome c - Cytochrome c        Peroxidase Complex
{'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 cytochrome c - cytochrome c peroxidase system provides an                   outstanding opportunity to uncover the intimate details of                      the structural requirements for peroxidase activity, as well                    as those for long range electron transfer between                               physiologically related heme proteins.  The objective of this                   research proposal is to elucidate the detailed mechanism of                     cytochrome c peroxidase catalysis with special emphasis on                      characterizing the interaction between cytochrome c and                         cytochrome c peroxidase.  Experiments designed to clarify the                   stoichiometry of binding between cytochrome c and cytochrome                    c peroxidase will be performed to determine if, and under                       what conditions, more than one cytochrome c may bind to                         cytochrome c peroxidase.  The specificity of binding at the                     high affinity binding site will be explored by utilizing a                      variety of cytochrome cs isolated from different sources and                    through site-directed mutagenesis of cytochrome c peroxidase.                   Transient state kinetic techniques will be used to                              investigate the rate of electron transfer between                               ferrocytochrome c and the oxidized intermediates of                             cytochrome c preoxidase.  The specificity of the reaction                       dynamics will be evaluated by using cytochrome c from various                   sources and the role of specific amino acid residues in the                     enzyme will be explored by site-directed mutagenesis.
{'FirstName': 'James', 'LastName': 'Erman', 'PI_MID_INIT': 'E', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'James E Erman', 'EmailAddress': 'jerman@niu.edu', 'NSF_ID': '000470653', 'StartDate': '04/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Northern Illinois University', 'CityName': 'DEKALB', 'ZipCode': '601152828', 'PhoneNumber': '8157531581', 'StreetAddress': '1425 W LINCOLN HWY', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Illinois', 'StateCode': 'IL', 'CONGRESSDISTRICT': '16', 'CONGRESS_DISTRICT_ORG': 'IL16', 'ORG_UEI_NUM': 'M2EEE68GGCY9', 'ORG_LGL_BUS_NAME': 'NORTHERN ILLINOIS UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
{'Name': None, 'CityName': None, 'StateCode': None, 'ZipCode': None, 'StreetAddress': None, 'CountryCode': None, 'CountryName': None, 'StateName': None, 'CountryFlag': None, 'CONGRESSDISTRICT': None, 'CONGRESS_DISTRICT_PERF': '""'}
{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8716459.xml'}