Electrochemistry of Strongly Adsorbed Heme Proteins
{'Code': '03090006', 'Directorate': {'Abbreviation': 'MPS', 'LongName': 'Direct For Mathematical & Physical Scien'}, 'Division': {'Abbreviation': 'CHE', 'LongName': 'Division Of Chemistry'}}
{'SignBlockName': 'Henry N. Blount, III', 'PO_EMAI': None, 'PO_PHON': None}
This project is in the general area of analytical and surface                   chemistry and in the subfields of bioelectrochemistry, electron                 transfer and modified electrodes.  A fundamental investigation                  of the interfacial electron transfer reactions of immobilized                   proteins that undergo oxidation-reduction reactions on                          electrodes will be undertaken. The results will help to                         elucidate the electronic coupling between enzymes and                           electronically conducting materials.  They will also provide                    insight into biological electron transfer processes as                          "protein/electrode complexes" can be considered analogues of                    physiological protein/protein complexes.  A variety of                          electrochemical and spectroscopic methods will be employed.                     Adsorption isotherms, protein orientation, adsorbate nativeness                 and electron transfer activation parameters will be determined.                 The heme proteins cytochrome c, cytochrome c552, and cytochrome                 c peroxidase, adsorbed on tin oxide electrodes, will be                         investigated to enable evaluation of the roles of electron                      transfer distance and electrostatic surface interactions as                     rate-controlling factors.                                                                                                                                       Systematic study of the electrochemical characteristics of                      adsorbed proteins that undergo oxidation-reduction reactions                    will aid in elucidating the role of electron transfer in                        biological systems.  The results will also aid in the design of                 efficient biological probes and sensors.
{'FirstName': 'Edmond', 'LastName': 'Bowden', 'PI_MID_INIT': 'F', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Edmond F Bowden', 'EmailAddress': 'edmond_bowden@ncsu.edu', 'NSF_ID': '000237625', 'StartDate': '08/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'North Carolina State University', 'CityName': 'RALEIGH', 'ZipCode': '276950001', 'PhoneNumber': '9195152444', 'StreetAddress': '2601 WOLF VILLAGE WAY', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'North Carolina', 'StateCode': 'NC', 'CONGRESSDISTRICT': '02', 'CONGRESS_DISTRICT_ORG': 'NC02', 'ORG_UEI_NUM': 'U3NVH931QJJ3', 'ORG_LGL_BUS_NAME': 'NORTH CAROLINA STATE 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': '1972', 'Text': 'ELECTROCHEMISTRY & SURFACE CHE'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8820832.xml'}