Oxygen-18 Exchange Studies of Energy Coupling in E1E2       Type ATPases
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Eve Ida Barak', 'PO_EMAI': None, 'PO_PHON': None}
A variety of life processes depend on the selective transport                   of ions across cell membranes against a concentration                           gradient.  Despite the importance of this phenomenon, the                       most fundamental questions about the molecular mechanism of                     active transport remain unanswered.  The objective of the                       proposed research is to learn how ion transport is coupled to                   catalysis of energy release from the biological storage                         molecule (ATP) by the class of enzyme that forms a                              phosphoenzyme intermediate (E1E2-type).  The current theory                     is that phosphorylation by ATP and by inorganic phosphate                       (P1) are catalyzed by different conformations of the enzyme.                    This idea will be tested by studying oxygen-18 exchange,                        which is catalyzed when the enzyme is phosphorylated.  The                      rate of appearance and disappearance of inorganic phosphate                     containing from zero to four oxygen-18 atoms can be measured                    by mass spectrometry or nuclear magnetic resonance.  The                        pattern of isotope exchange depends upon the mehcanism of the                   reaction.  It has been found to change dramatically when the                    concentration of one of the ions transported by the proton,                     potassium-ATPase (H+) is increased.  Therefore, the                             relationship between conformational state and mechanism can                     be sensitively probed by measuring the isotope exchange                         pattern.  The enzyme that catalyzes sodium, potassium                           transport will also be studied, because there is a wealth of                    information on how Na+ and K+ affect the conformation of the                    enzyme.  The primary model to be used in these studies, the                     gastric proton, potassium-ATPase, is important                                  physiologically as well as theoretically.
{'FirstName': 'Larry', 'LastName': 'Faller', 'PI_MID_INIT': 'D', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Larry D Faller', 'EmailAddress': None, 'NSF_ID': '000291491', 'StartDate': '09/01/1987', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-Los Angeles', 'CityName': 'LOS ANGELES', 'ZipCode': '900244200', 'PhoneNumber': '3107940102', 'StreetAddress': '10889 WILSHIRE BLVD STE 700', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '36', 'CONGRESS_DISTRICT_ORG': 'CA36', 'ORG_UEI_NUM': 'RN64EPNH8JC6', 'ORG_LGL_BUS_NAME': 'UNIVERSITY OF CALIFORNIA, LOS ANGELES', 'ORG_PRNT_UEI_NUM': None}
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1987&All=true', 'xml': '8704525.xml'}