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Article

Reaction of N-hydroxyguanidine with the ferrous-oxy state of a heme peroxidase cavity mutant: a model for the reactions of nitric oxide synthase.

Archives of biochemistry and biophysics - 1 Aug 2010

Nigro Alycen Pond, Goodin David B

Abstract excerpt

Yeast cytochrome c peroxidase was used to construct a model for the reactions catalyzed by the second cycle of nitric oxide synthase. The R48A/W191F mutant introduced a binding site for N-hydroxyguanidine near the distal heme face and removed the redox active Trp-191 radical site. Both the R48A and R48A/W191F mutants catalyzed the H2O2 dependent conversion of N-hydroxyguanidine to N-nitrosoguanidine. It is...

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Identifiers

PMID: 20346907
DOI: 10.1016/j.abb.2010.03.012
PMCID: PMC2902621

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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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