Cited by 13Hemoglobin structure and functionMetal-Catalyzed Oxygenation MechanismsMetalloenzymes and iron-sulfur proteins

Nitrite reduction: a ubiquitous function from a pre-aerobic past

Cutruzzolà, Francesca, Rinaldo, Serena, Castiglione, Nicoletta, Giardina, Giorgio, Pecht, Israel, Brunori, Maurizio·2009·BioEssays

Abstract

In eukaryotes, small amounts of nitrite confer cytoprotection against ischemia/reperfusion-related tissue damage in vivo, possibly via reduction to nitric oxide (NO) and inhibition of mitochondrial function. Several hemeproteins are involved in this protective mechanism, starting with deoxyhemoglobin, which is capable of reducing nitrite. In facultative aerobic bacteria, such as Pseudomonas aeruginosa, nitrite is reduced to NO by specialized heme-containing enzymes called cd(1) nitrite reductases. The details of their catalytic mechanism are summarized below, together with a hypothesis on the biological role of the unusual d(1)-heme, which, in the reduced state, shows unique properties (very high affinity for nitrite and exceptionally fast dissociation of NO). Our results support the idea that the nitrite-based reactions of contemporary eukaryotes are a vestige of earlier bacterial biochemical pathways. The evidence that nitrite reductase activities of enzymes with different cellular roles and biochemical features still exist today highlights the importance of nitrite in cellular homeostasis.

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Crossref · 10.1002/bies.200800235

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75 of 75 references verified0 citation errors · 0 not checkable

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  • Eukaryotic cells employ enzymatic nitrite reduction.

    “While it has been well known that prokaryotes contain numerous nitrite/nitrate reductases, the confirmation that eukaryotic cells employ enzymatic nitrite reduction has only recently become clear [129].”

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Authors
Cutruzzolà, F., Rinaldo, S., Castiglione, N., Giardina, G., Pecht, I., & Brunori, M.
Affiliations
  • Sapienza University of Rome (IT)
  • Weizmann Institute of Science (IL)
Corresponding author
Cutruzzolà, Francesca
Venue
BioEssays
Publisher
Wiley
Published
2009-07-16
Volume
31
Issue
8
Pages
885-891
ISSN
  • 0265-9247 (ISSN-L)
  • 1521-1878
OpenAlex
W2017543986
Cited by
13
References
75
Citations by year
2017: 1 · 2015: 2 · 2014: 1 · 2013: 1 · 2012: 4
FWCI
0.20
Type
journal article
Language
en
Open access
closed
Locations
  • BioEssays (publishedVersion)
  • PubMed (publishedVersion)
  • IRIS Research product catalog (Sapienza University of Rome) (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords
nitrite reduction, nitric oxide, deoxyhemoglobin, mitochondrial function, Pseudomonas aeruginosa, catalytic mechanism
MeSH terms
Aerobiosis, Bacteria, Eukaryotic Cells, Nitric Oxide, Nitrites, Oxidation-Reduction

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