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Model complexes of key intermediates in fungal cytochrome P450 nitric oxide reductase (P450nor)

Authors
  • McQuarters, Ashley B
  • Wirgau, Nathaniel E
  • Lehnert, Nicolai1
  • 1 Department of Chemistry, University of Michigan
Type
Published Article
Journal
Current Opinion in Chemical Biology
Publisher
Elsevier
Publication Date
Jan 01, 2014
Volume
19
Pages
82–89
Identifiers
DOI: 10.1016/j.cbpa.2014.01.017
Source
Elsevier
License
Unknown

Abstract

Denitrifying bacteria and fungi efficiently detoxify the toxic metabolite nitric oxide (NO) through reduction to nitrous oxide (N2O) using nitric oxide reductase (NOR) enzymes. In fungi, for example Fusarium oxysporum, NO is reduced by a Cytochrome P450 NOR (P450nor). This enzyme contains a heme b center coordinated to a proximal cysteinate ligand in the active site. In the proposed mechanism of P450nor, the ferric heme binds NO first to form a ferric heme-nitrosyl complex, which is subsequently reduced by NAD(P)H to generate a ferrous HNO species as the next key intermediate. Recently, key progress has been made in our understanding of the electronic structures and fundamental reactivity of these important intermediates, using suitable model complexes. In this review, model complexes of ferric heme-nitrosyls with varied axial anionic ligands (such as N-donors, O-donors, and S-donors) are discussed first. Then, the generation and reactivity of ferrous heme-HNO complexes is summarized and related back to the mechanism of P450nor.

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