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

B. S.S. Masters, K. Mcmillan, E. A. Sheta, J. S. Nishimura, L. J. Roman, P. Martasek

Research output: Contribution to journalReview article

191 Scopus citations

Abstract

The nitric oxide synthases (NOS-I, neuronal, NOS-II, inducible, and NOS-III, endothelial) are the most recent additions to the large number of heme proteins that contain cysteine thiolate-liganded protoporphyrin IX heme prosthetic groups. This group of oxygenating enzymes also includes one of the largest gene families, that of the cytochromes P450, which have been demonstrated to be involved in the hydroxylation of a variety of substrates, including endogenous compounds (steroids, fatty acids, and prostaglandins) and exogenous compounds (therapeutic drugs, environmental toxicants, and carcinogens). The substrates for cytochromes P450 are universally hydrophobic while the physiological substrate for the nitric oxide synthases is the amino acid L-arginine, a hydrophilic compound. This review will discuss the approaches being used to study the structure and mechanism of neuronal nitric oxide synthase in the context of its known prosthetic groups and regulation by Ca2+-calmodulin and/or tetrahydrobiopterin (BH4).

Original languageEnglish (US)
Pages (from-to)552-558
Number of pages7
JournalFASEB Journal
Volume10
Issue number5
DOIs
StatePublished - Apr 1996

Keywords

  • Ca-calmodulin
  • Cysteine thiolate-bound heme
  • FAD and FMN
  • L-arginine
  • L-citrulline
  • Modular structure
  • NO•
  • Tetrahydrobiopterin

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics

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