A cross-domain charge interaction governs the activity of NO synthase-Reference-Cited by-同舟云学术

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A cross-domain charge interaction governs the activity of NO synthase

Published:2018-03 Issue:12 Volume:293 Page:4545-4554
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Haque Mohammad Mahfuzul,Tejero Jesús,Bayachou Mekki,Kenney Claire T.,Stuehr Dennis J.

Funder

HHS NIH National Institute of General Medical Sciences (NIGMS)

HHS NIH National Institute of Biomedical Imaging and Bioengineering (NIBIB)

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference51 articles.

1. Nitric oxide synthases: properties and catalytic mechanism;Griffith;Annu. Rev. Physiol,1995

2. NO synthase: structures and mechanisms;Daff;Nitric Oxide,2010

3. Neuronal nitric oxide synthase, a modular enzyme formed by convergent evolution: structure studies of a cysteine thiolate-liganded heme protein that hydroxylates l-arginine to produce NO as a cellular signal;Masters;FASEB J,1996

4. Enzymatic function of nitric oxide synthases;Andrew;Cardiovasc. Res,1999

5. Tetrahydrobiopterin radical enzymology;Wei;Chem. Rev,2003

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