作者: Samantha J.O. Hardman , Christopher R. Pudney , Sam Hay , Nigel S. Scrutton
DOI: 10.1016/J.BPJ.2013.10.015
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摘要: In enzyme systems where fast motions are thought to contribute H-transfer efficiency, the distance between hydrogen donor and acceptor is a very important factor. Sub-angstrom changes in donor-acceptor can have large effect on rate of reaction, so sensitive probe these vital tool our understanding function. this study we use ultrafast transient absorption spectroscopy investigate photoinduced electron transfer rates, which also small distance, coenzyme analog, NAD(P)H4, isoalloxazine center model flavoenzymes morphinone reductase (wild-type selected variants) pentaerythritol tetranitrate (wild-type). It shown that upon addition protein increased. By comparing magnitude increase with existing values for NAD(P)H4-FMN distances, based charge-transfer complex absorbance experimental kinetic isotope reaction data, show method be used as range systems.