中国科技核心期刊
CN:31-1600/Q
ISSN:1004-0374
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《生命科学》 2011, 23(8): 790-795
一氧化氮合酶FMN结合结构域的电子传递及调控机制研究现状
王瑞勇,张 璐,柴亚辉,吴 静,尹瑜静,常俊标*
(郑州大学化学系,郑州 45000)
摘 要:生物体内NO是在一氧化氮合酶(mitric oxide synthase, NOS)催化下生成的,NOS的结构包括C端还原酶域和N端加氧酶域。还原酶域中的FMN结合结构域既可接受来自NADPH-FAD结构域的电子,又可作为提供电子的供体,在调控催化过程中的电子传递方面发挥着重要作用。主要从FMN结合结构域的构象平衡及其对不同亚型NOS的动力学差异的贡献、FMN结合结构域自身的电荷性质以及NOS中其他结构域对FMN结构域的功能调控三个方面进行了论述,以期揭示NOS独特的电子传递催化机制。
关键词:一氧化氮合酶; FMN结合结构域; 电子传递
 
Electron transfer and regulation mechanism of FMN subdomain in nitric oxide synthase
WANG Rui-Yong, ZHANG Lu, CHAI Ya-Hui, WU Jing, YIN Yu-Jing, CHANG Jun-Biao*
(Department of Chemistry, Zhengzhou University, Zhengzhou 450001, China)
Abstract: NO synthesis in vivo is catalyzed by nitric oxide synthase. Nitric-oxide synthase is composed of a C-terminal, flavin-containing reductase domain and an N-terminal, heme-containing oxidase domain. FMN domain plays a central role by acting as both an electron acceptor (receiving electrons from NADPH-FAD) and an electron donor (delivering electrons to the NOS heme). In the minireview, the following sections were presented: (i) a three-state, two-equilibrium model for the conformation of the FMN subdomain, in addition, its contribution to differences of nitric-oxide synthases I, II, and III from the view of kinetic, (ii) the surface charge of the FMN subdomain, (iii) how the partner subdomain (C-terminal residue and CaM binding) regulate the conformational equilibria of the FMN module in NOS. This helps to explain the unique electron transfer and catalytic behaviors of NOS.
Key words: nitric oxide synthase; FMN domain; electron transfer
 
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