NO synthase: Structures and mechanisms

Research output: Contribution to journalLiterature reviewpeer-review

Abstract / Description of output

Production of NO from arginine and molecular oxygen is a complex chemical reaction unique to biology. Our understanding of the chemical and regulation mechanisms of the NO synthases has developed over the past two decades, uncovering some extraordinary features. This article reviews recent progress and highlights current issues and controversies. The structure of the enzyme has now been determined almost in entirety, although it is as a selection of fragments, which are difficult to assemble unambiguously. NO synthesis is driven by electron transfer through FAD and FMN cofactors, which is controlled by calmodulin binding in the constitutive mammalian enzymes. Many of the unique structural features involved have been characterised, but the mechanics of calmodulin-dependent activation are largely unresolved. Ultimately, NO is produced in the active site by the reaction of arginine with activated heme-bound oxygen in two distinct cycles. The unique role of the tetrahydrobiopterin cofactor as an electron donor in this process has now been established, but the subsequent chemical events are currently a matter of intense speculation and debate. (C) 2010 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)111
Number of pages11
JournalNitric Oxide
Volume23
Issue number1
DOIs
Publication statusPublished - 1 Aug 2010

Keywords / Materials (for Non-textual outputs)

  • Nitric oxide
  • NOS
  • Monooxygenation
  • Calmodulin
  • Flavin
  • Heme
  • NITRIC-OXIDE SYNTHASE
  • INTRAPROTEIN ELECTRON-TRANSFER
  • L-ARGININE
  • REDUCTASE DOMAIN
  • CYTOCHROME-P450 REDUCTASE
  • CONFORMATIONAL EQUILIBRIUM
  • FLAVOCYTOCHROME P450BM3
  • CALMODULIN-BINDING
  • OXYGEN ACTIVATION
  • BACILLUS-SUBTILIS

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