Cytochrome P-450-CO and substrates:: lessons from ligand binding under high pressure

被引：24

作者：

Jung, C ^{[1
]}

机构：

[1] Max Delbruck Ctr Mol Med, Prot Dynam Lab, D-13125 Berlin, Germany

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2002年 / 1595卷 / 1-2期

关键词：

high pressure; cytochrome P-450; ligand binding; Fourier transform infrared spectroscopy; UV-visible spectroscopy; compressibility;

D O I：

10.1016/S0167-4838(01)00353-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An overview of the application of high-pressure studies on the carbon monoxide complex of cytochrome P-450 is given. Different approaches to characterize ligand binding steps, the conformational states and substates and the compressibility of the ligand-bound complex are reviewed. A particular focus is the effect of substrates on these properties. It is shown that substrate mobility, compressibility and water accessibility are interrelated and may have functional meaning. (C) 2002 Elsevier Science B.V. All rights reserved.

引用

页码：309 / 328

页数：20

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