Importance of Val567 on heme environment and substrate recognition of neuronal nitric oxide synthase-Reference-Cited by-同舟云学术

Importance of Val567 on heme environment and substrate recognition of neuronal nitric oxide synthase

Published:2018-08-20 Issue:9 Volume:8 Page:1553-1566
ISSN:2211-5463
Container-title:FEBS Open Bio
language:en
Short-container-title:FEBS Open Bio

Author:

Olsbu Inger K.¹,Zoppellaro Giorgio²,Andersson K. Kristoffer¹,Boucher Jean‐Luc³,Hersleth Hans‐Petter¹⁴^ORCID

Affiliation:

1. Department of Biosciences Section for Biochemistry and Molecular Biology University of Oslo Norway

2. Regional Centre of Advanced Technologies and Materials Department of Physical Chemistry Faculty of Science Palacky University in Olomouc Czech Republic

3. UMR 8601CNRS‐University Paris Descartes France

4. Department of Chemistry Section for Chemical Life Sciences University of Oslo Norway

Funder

Norges Forskningsråd

Publisher

Wiley

Subject

General Biochemistry, Genetics and Molecular Biology

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/2211-5463.12503

Reference65 articles.

1. Nitric oxide synthases: structure, function and inhibition

2. NO synthase: Structures and mechanisms

3. Nitric oxide synthases domain structure and alignment in enzyme function and control

4. Calmodulin controls neuronal nitric‐oxide synthase by a dual mechanism. Activation of intra‐ and interdomain electron transfer;Abu‐Soud HM;J Biol Chem,1994

5. 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

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