Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 126, Issue 46, Pages 15120-15131Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja047050e
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- NIGMS NIH HHS [GM 25765, GM 20709] Funding Source: Medline
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Apo-glucose oxidase has been reconstituted with flavins modified in the 7 and 8 positions and characterized with regard to the catalytic rate of O-2 reduction and oxygen-18 isotope effects on this process. Kinetic studies as a function of driving force indicate a reorganization energy for electron transfer to 02 Of lambda=28 kcal mol(-1) at optimal pH, which is similar to the value obtained earlier from temperature dependencies of rates (Roth, J. P.; Klinman, J. P. Proc. Nad. Acad. Sci. U.S.A. 2003, 100, 62-67). For the various enzyme-bound flavins, competitive oxygen-18 kinetic isotope effects fall within the narrow range of 1.0266(5) to 1.0279(6), apparently because of the dominant contribution of outer-sphere reorganization to the activation barrier; within the context of semiclassical and quantum mechanical electron transfer theories, the magnitude of the isotope effects reveals the importance of nuclear tunneling.
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