Flavocytochrome c: A Model for Coupled Electron Transfer
{'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}
Flavocytochrome c will be investigated further as a soluble                     model of oriented coupled electron transfer.  The heme and                      flavin  subunits are tightly associated and it has been shown                   that electron flow is from doner to flavin, followed by rapid                   intramolecular transfer to the heme and finally to the                          acceptor.  The flavin and heme are optimally oriented for                       electron transfer and the electrons enter and exit via                          different paths.  Flavocytrochrome c will be cloned and the                     mechanism of electron transfer will be further characterized.                                                                                                   Considerable advances in our knowledge of biological electron                   transfer have been achieved, although many crucial questions                    remain unanswered.  Much of our present understanding is based                  on studies with cytochrome c (the only soluble protein in the                   respiratory chain) and other small proteins having a single                     redox center.  It is clear that redox potential, electrostatic                  and steric factors play an important role.  In larger proteins                  containing multiple redox centers these interactions are less                   well understood, but additional factors play a role.  Thus the                  mechanism of action of cytochrome c may not be representative                   as a whole.  Flavocytchrome c  presents an opportunity to                       investigate an electron transfer system which more directly                     mimics the less tractable membrane found electron carriers of                   respiratory and photosynthetic pathways.
[{'FirstName': 'Terrance', 'LastName': 'Meyer', 'PI_MID_INIT': 'E', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Terrance E Meyer', 'EmailAddress': 'temeyer@u.arizona.edu', 'NSF_ID': '000470813', 'StartDate': '08/01/1988', 'EndDate': None, 'RoleCode': 'Co-Principal Investigator'}, {'FirstName': 'Michael', 'LastName': 'Cusanovich', 'PI_MID_INIT': 'A', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Michael A Cusanovich', 'EmailAddress': 'cusanovi@u.arizona.edu', 'NSF_ID': '000468183', 'StartDate': '08/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}]
{'Name': 'University of Arizona', 'CityName': 'TUCSON', 'ZipCode': '85721', 'PhoneNumber': '5206266000', 'StreetAddress': '845 N PARK AVE RM 538', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Arizona', 'StateCode': 'AZ', 'CONGRESSDISTRICT': '07', 'CONGRESS_DISTRICT_ORG': 'AZ07', 'ORG_UEI_NUM': 'ED44Y3W6P7B9', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF ARIZONA', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '114400', 'Text': 'Molecular Biophysics'}
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