Physiochemical Studies on Xanthine Oxidizing Enzymes
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Kamal Shukla', 'PO_EMAI': None, 'PO_PHON': None}
Dr. Massey is continuing his study of milk xanthine oxidase                     in which the chemical, physical and structural properties of                    the four redox centers of the enzyme and the interactions                       between them will be examined.  The project will also include                   a comparative study with two closely related enzymes, the                       dehydrogenase form of the milk enzyme and the stable xanthine                   dehydrogenase from chicken liver.  Major use will be made of                    stopped flow optical techniques to monitor oxidation and                        reduction of the redox centers under various conditions as                      well as extensive use of 13C NMR to study the interaction of                    substrates, products and inhibitors with the molybdenum                         center.                                                                                                                                                         Xanthine oxidase is a well-studied molybdenum-containing                        hydroxylase and studies on the enzyme lie at the forefront                      of our efforts to establish the structure of the molybdenum                     centers and the chemical mechanisms operative in this small                     but important class of enzymes.  Because xanthine oxidase                       contains no fewer than four centers capable of reversibly                       taking up reducing equivalents, the enzyme also serves as a                     useful model for the interaction of redox-active centers in                     the more complicated systems of photosynthetic and                              mitochondrial electron transport. ***
{'FirstName': 'Vincent', 'LastName': 'Massey', 'PI_MID_INIT': None, 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Vincent Massey', 'EmailAddress': None, 'NSF_ID': '000329263', 'StartDate': '11/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Regents of the University of Michigan - Ann Arbor', 'CityName': 'ANN ARBOR', 'ZipCode': '481091079', 'PhoneNumber': '7347636438', 'StreetAddress': '1109 GEDDES AVE, SUITE 3300', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'Michigan', 'StateCode': 'MI', 'CONGRESSDISTRICT': '06', 'CONGRESS_DISTRICT_ORG': 'MI06', 'ORG_UEI_NUM': 'GNJ7BBP73WE9', 'ORG_LGL_BUS_NAME': 'REGENTS OF THE UNIVERSITY OF MICHIGAN', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1164', 'Text': 'MOLECULAR BIOPHYSICS'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8803843.xml'}