Mechanistic Studies on the Lactate Dehydrogenase Reaction
{'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}
Lactate dehydrogenase catalyzes the oxidation of lactate by                     facilitating the direct, simultaneous transfer of a proton and                  two electrons to the coenzyme, NAD+.  Because many other                        dehydrogenases operate in a similar manner, the proposed                        research serves as a model for future explanations of how                       dehydrogenases accomplish large accelerations of chemical                       reactions.  Using both chemical kinetics and Raman spectroscopy                 to determine changes in the chemical bonds of both the                          substrate and coenzyme upon binding to the enzyme, these                        changes to the structure, which is known, of the enzyme with                    substrate and coenzyme bound will be related.  These studies                    will partially involve the synthesis of isotopically labeled                    substrates and coenzymes so that Raman bands can be assigned to                 the molecular motions of these molecules both  in solution and                  bound to enzyme.  These studies also will be extended to                        formate dehydrogenase to produce a more general picture of the                  interactions that occur.                                                                                                                                        Recent work shows that to a large extent enzymes use                            noncovalent interactions to facilitate the making and breaking                  of covalent bonds and to make or break them sterically.                         Because the energies of noncovalent interactions are not easily                 assessed during an enzyme reaction a description of the                         contributions to enzyme catalysis provided by various types of                  noncovalent interactions is a difficult yet important goal, and                 the possibility of rationalizing enzymic reactions in terms of                  the observed rate effects produced by simple catalysts has been                 the goal of enzyme chemists for many years.  Because of this                    work this may be possible for NAD dependent dehydrogenasis.
[{'FirstName': 'John', 'LastName': 'Burgner', 'PI_MID_INIT': 'W', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'John W Burgner', 'EmailAddress': None, 'NSF_ID': '000293388', 'StartDate': '02/15/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}, {'FirstName': 'William', 'LastName': 'Ray', 'PI_MID_INIT': 'J', 'PI_SUFX_NAME': 'Jr.', 'PI_FULL_NAME': 'William J Ray', 'EmailAddress': None, 'NSF_ID': '000267229', 'StartDate': '02/15/1989', 'EndDate': None, 'RoleCode': 'Co-Principal Investigator'}]
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{'Code': '1144', 'Text': 'Molecular Biophysics'}
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