Cited by 160Nitric Oxide and Endothelin EffectsHemoglobin structure and functionMetal-Catalyzed Oxygenation Mechanisms

Bacterial nitric oxide synthases: what are they good for?

Sudhamsu, Jawahar, Crane, Brian R.·2009·Trends in Microbiology

Abstract

Nitric oxide synthases (NOSs) are heme-based monooxygenases that oxidize L-arginine to nitric oxide (NO), a signaling molecule and cytotoxic agent in higher organisms. Although NOS-like activity has been reported in many bacteria, only a few bacterial homologs of mammalian NOSs (mNOSs) have been characterized to date. In contrast to mNOSs, which possess both a catalytic and a reductase domain, the bacterial enzymes lack reductase domains and require the supply of suitable reductants to produce NO. A notable exception is a NOS from a gram-negative bacterium that contains a new type of reductase module. Remarkably, bacterial NOSs seem to have functions that differ from those of mNOSs, including nitration of different metabolites and protection against oxidative stress. Studies of bacterial NOSs will probably result in a better understanding of the mechanism of NO synthesis and unveil a variety of new functions for NO in microbes.

Integrity signals

Registry

Crossref · 10.1016/j.tim.2009.02.003

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The citation lists haven’t been fetched yet

References 59 · Cited by 160

Authors
Sudhamsu, J., & Crane, B. R.
Affiliations
Cornell University (US)
Corresponding author
Crane, Brian R.
Venue
Trends in Microbiology
Publisher
Elsevier BV
Published
2009-05
Volume
17
Issue
5
Pages
212-218
ISSN
0966-842X (ISSN-L)
OpenAlex
W1998904566
Cited by
160
References
59
Citations by year
2026: 3 · 2025: 7 · 2024: 9 · 2023: 3 · 2022: 7 · 2021: 8 · 2020: 5 · 2019: 10 · 2018: 13 · 2017: 11 · 2016: 15 · 2015: 7 · 2014: 14 · 2013: 4 · 2012: 14
FWCI
1.61
Type
journal article
Language
en
Open access
closed
Locations
  • Trends in Microbiology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Keywords
nitric oxide production, L-arginine oxidation, heme monooxygenase, reductase domain, antioxidant defense, Gram-negative bacteria
MeSH terms
Arginine, Bacteria, Bacterial Proteins, Nitric Oxide, Oxidation-Reduction, Stress, Physiological, Oxidative Stress, Bacterial Physiological Phenomena, Nitric Oxide Synthase

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review