Spring-loading the active site of cytochrome P450cam

被引：12

作者：

Dang, Marina ^{[1
]}

Pochapskya, Susan Sondej ^{[1
]}

Pochapsky, Thomas C. ^{[1
,2
]}

机构：

[1] Brandeis Univ, Dept Chem, Waltham, MA 02454 USA

[2] Brandeis Univ, Rosenstiel Basic Med Sci Res Inst, Waltham, MA 02454 USA

来源：

METALLOMICS | 2011年 / 3卷 / 04期

基金：

美国国家卫生研究院;

关键词：

CRYSTAL-STRUCTURE; STRUCTURAL BASIS; SUBSTRATE; SPECIFICITY; RECOGNITION; MODEL; SPIN;

D O I：

10.1039/c0mt00065e

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：

A hydrogen bond network has been identified that adjusts protein-substrate contacts in cytochrome P450(cam) (CYP101A1). Replacing the native substrate camphor with adamantanone or norcamphor causes perturbations in NMR-detected NH correlations assigned to the network, which includes portions of a beta sheet and an adjacent helix that is remote from the active site. A mutation in this helix reduces enzyme efficiency and perturbs the extent of substrate-induced spin state changes at the haem iron that accompany substrate binding. In turn, the magnitude of the spin state changes induced by alternate substrate binding parallel the NMR-detected perturbations observed near the haem in the enzyme active site.

引用

页码：339 / 343

页数：5

共 21 条

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