The cytochrome cbb3 from Pseudomonas stutzeri displays nitric oxide reductase activity

Elena Forte, Andrea Urbani, Matti Saraste, Paolo Sarti, Maurizio Brunori, Alessandro Giuffrè

Research output: Contribution to journalArticle

Abstract

The cytochrome cbb3 is an isoenzyme in the family of cytochrome c oxidases. This protein purified from Pseudomonas stutzeri displays a cyanide-sensitive nitric oxide reductase activity (Vmax = 100 ± 9 mol NO·mol cbb3 -1·min-1 and Km = 12 ± 2.5 μM), which is lost upon denaturation. This enzyme is only partially reduced by ascorbate, and readily re-oxidized by NO under anaerobic conditions at a rate consistent with the turnover number for NO consumption. As shown by transient spectroscopy experiments and singular value decomposition (SVD) analysis, these results suggest that the cbb3-type cytochromes, sharing structural features with bacterial nitric oxide reductases, are the enzymes retaining the highest NO reductase activity within the heme-copper oxidase superfamily.

Original languageEnglish
Pages (from-to)6486-6490
Number of pages5
JournalEuropean Journal of Biochemistry
Volume268
Issue number24
DOIs
Publication statusPublished - 2001

Keywords

  • Denitrifying bacteria
  • Evolution
  • Respiration
  • Spectroscopy

ASJC Scopus subject areas

  • Biochemistry

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