期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 55, 期 32, 页码 9361-9364出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201603592
关键词
biocatalysis; enzymes; hydrostatic pressure; protein conformations; protein motions
资金
- National Institutes of Health [GM118117-01]
The proposed contributions of distinct classes of local versus global protein motions during enzymatic bond making/breaking processes has been difficult to verify. We employed soybean lipoxygenase-1 as a model system to investigate the impact of high pressure at variable temperatures on the hydrogen-tunneling properties of the wild-type protein and three single-site mutants. For all variants, pressure dramatically elevates the enthalpies of activation for the C-H activation. In contrast, the primary kinetic isotope effects (KIEs) for C-H activation and their corresponding temperature dependencies remain unchanged up to ca. 700 bar. The differential impact of elevated hydrostatic pressure on the temperature dependencies of rate constants versus substrate KIEs provides direct evidence for two distinct classes of protein motions: local, isotope-dependent donor-acceptor distance-sampling modes, and a more global, isotope-independent search for productive protein conformational sub-states.
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