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Article

Comparison of wild type neuronal nitric oxide synthase and its Tyr588Phe mutant towards various L-arginine analogues.

Journal of inorganic biochemistry - 1 Oct 2010

Giroud Claire, Moreau Magali, Sagami Ikuko, Shimizu Toru, Frapart Yves, Mansuy Daniel, Boucher Jean-Luc

Abstract excerpt

Crystal structures of nitric oxide synthases (NOS) isoforms have shown the presence of a strongly conserved heme active-site residue, Tyr588 (numbering for rat neuronal NOS, nNOS). Preliminary biochemical studies have highlighted its importance in the binding and oxidation to NO of natural substrates L-Arg and N(omega)-hydroxy-L-arginine (NOHA) and suggested its involvement in mechanism. We have used UV-visible...

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PMID: 20630600
DOI: 10.1016/j.jinorgbio.2010.06.001

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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