Holoenzyme structures of endothelial nitric oxide synthase – An allosteric role for calmodulin in pivoting the FMN domain for electron transfer-Reference-Cited by-同舟云学术

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Holoenzyme structures of endothelial nitric oxide synthase – An allosteric role for calmodulin in pivoting the FMN domain for electron transfer

Published:2014-10 Issue:1 Volume:188 Page:46-54
ISSN:1047-8477
Container-title:Journal of Structural Biology
language:en
Short-container-title:Journal of Structural Biology

Author:

Volkmann Niels,Martásek Pavel,Roman Linda J.,Xu Xiao-Ping,Page Christopher,Swift Mark,Hanein Dorit,Masters Bettie Sue

Funder

NIH

Robert A. Welch Distinguished Chair in Chemistry

Charles University

European Regional Development Fund

Publisher

Elsevier BV

Subject

Structural Biology

Reference59 articles.

1. Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase;Aigrain;EMBO Rep.,2009

2. Nitric oxide synthases: structure, function and inhibition;Alderton;Biochem. J.,2001

3. Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase;Astashkin;J. Am. Chem. Soc.,2010

4. The reduction potential of nitric oxide (NO) and its importance to NO biochemistry;Bartberger;Proc. Natl. Acad. Sci. U.S.A.,2002

5. Nitric oxide: a physiologic messenger molecule;Bredt;Annu. Rev. Biochem.,1994

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