A perspective on conformational control of electron transfer in nitric oxide synthases

被引：19

作者：

Hedison, Tobias M. ^{[1
]}

Hay, Sam ^{[1
]}

Scrutton, Nigel S. ^{[1
]}

机构：

[1] Univ Manchester, Manchester Inst Biotechnol, Manchester, Lancs, England

来源：

NITRIC OXIDE-BIOLOGY AND CHEMISTRY | 2017年 / 63卷

基金：

英国生物技术与生命科学研究理事会; 英国工程与自然科学研究理事会;

关键词：

Nitric oxide synthase; Cytochrome P450 reductase; Diflavin oxidoreductase; Fluorescence; Protein dynamics; HUMAN CYTOCHROME-P450 REDUCTASE; AUTOINHIBITORY CONTROL ELEMENT; LASER FLASH-PHOTOLYSIS; FREE-ENERGY LANDSCAPE; CRYSTAL-STRUCTURE; HEME DOMAINS; FMN DOMAIN; FLAVOPROTEIN DOMAIN; 2-DOMAIN CONSTRUCT; CATALYTIC CYCLE;

D O I：

10.1016/j.niox.2016.09.002

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：

This perspective reviews single molecule and ensemble fluorescence spectroscopy studies of the three tissue specific nitric oxide synthase (NOS) isoenzymes and the related diflavin oxidoreductase cyto chrome P450 reductase. The focus is on the role of protein dynamics and the protein conformational landscape and we discuss how recent fluorescence-based studies have helped in illustrating how the nature of the NOS conformational landscape relates to enzyme turnover and catalysis. (C) 2016 The Authors. Published by Elsevier Inc.

引用

页码：61 / 67

页数：7

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