The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Nitric oxide dioxygenase: An enzymic function for flavohemoglobin
Open accessAbstract
Nitric oxide (NO • ) is a toxin, and various life forms appear to have evolved strategies for its detoxification. NO • -resistant mutants of Escherichia coli were isolated that rapidly consumed NO • . An NO • -converting activity was reconstituted in extracts that required NADPH, FAD, and O 2 , was cyanide-sensitive, and produced NO 3 − . This nitric oxide dioxygenase (NOD) contained 19 of 20 N-terminal amino acids identical to those of the E. coli flavohemoglobin. Furthermore, NOD activity was produced by the flavohemoglobin gene and was inducible by NO • . Flavohemoglobin/NOD-deficient mutants were also sensitive to growth inhibition by gaseous NO • . The results identify a function for the evolutionarily conserved flavohemoglobins and, moreover, suggest that NO • detoxification may be a more ancient function for the widely distributed hemoglobins, and associated methemoglobin reductases, than dioxygen transport and storage.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Analysis of nitrate, nitrite, and [15N]nitrate in biological fluids
Green, L. C., Wagner, D. A., Glogowski, J., Skipper, P. L., Wishnok, J. S., & Tannenbaum, S. R. (1982) · Analytical Biochemistry · doi:10.1016/0003-2697(82)90118-x · Cited by 12,077
The chemistry of peroxynitrite: A product from the reaction of nitric oxide with superoxide
Pryor, W. A., & Squadrito, G. L. (1995) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.1995.268.5.l699 · Cited by 1,511
Nitric oxide synthase structure and mechanism
Marletta, M. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31375-9 · Cited by 1,338
The Generation of Superoxide Radical during the Autoxidation of Hemoglobin
Misra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44679-6 · Cited by 1,174
Fang, F. C. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119473 · Cited by 1,149
Biological Roles of Nitric Oxide
Snyder, S. H., & Bredt, D. S. (1992) · Scientific American · doi:10.1038/scientificamerican0592-68 · Cited by 721
Control of coronary vascular tone by nitric oxide.
Kelm, M., & Schrader, J. (1990) · Circulation Research · doi:10.1161/01.res.66.6.1561 · Cited by 701
Oxidation of nitrogen-oxides by bound dioxygen in hemoproteins
Doyle, M. P., & Hoekstra, J. W. (1981) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80291-3 · Cited by 643
Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
WEISS, J. J. (1964) · Nature · doi:10.1038/202083b0 · Cited by 416
EPR characterization of molecular targets for NO in mammalian cells and organelles
Henry, Y., Lepoivre, M., Drapier, J., Ducrocq, C., Boucher, J., & Guissani, A. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.12.8397130 · Cited by 370
Cited by
Nathan, C., & Shiloh, M. U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.8841 · Cited by 1,469
Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity
Bogdan, C., Röllinghoff, M., & Diefenbach, A. (2000) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)00052-7 · Cited by 939
Nitric oxide signalling in plants
Neill, S. J., Desikan, R., & Hancock, J. T. (2003) · New Phytologist · doi:10.1046/j.1469-8137.2003.00804.x · Cited by 874
Pseudomonas aeruginosa Anaerobic Respiration in Biofilms
Yoon, S. S., Hennigan, R. F., Hilliard, G. M., Ochsner, U. A., Parvatiyar, K., Kamani, M. C., Allen, H. L., DeKievit, T. R., Gardner, P. R., Schwab, U., et al. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00295-2 · Cited by 585
Self-citationDynamic Gut Microbiome across Life History of the Malaria Mosquito Anopheles gambiae in Kenya
Wang, Y., Gilbreath, T. M., Kukutla, P., Yan, G., & Xu, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024767 · Cited by 584
Metadata
- Authors
- Gardner, P. R., Gardner, A. M., Martin, L. A., & Salzman, A. L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-09
- Volume
- 95
- Issue
- 18
- Pages
- 10378-10383
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2133709520
- Cited by
- 565
- References
- 44
- FWCI
- 6.90
- Type
- journal article
- Language
- en
- Open access
- green
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Nitric oxide dioxygenase: An enzymic function for flavohemoglobin. https://app.cochat.ai/papers/10.1073/pnas.95.18.10378
- The paper
- Gardner, P. R., Gardner, A. M., Martin, L. A., & Salzman, A. L. (1998). Nitric oxide dioxygenase: An enzymic function for flavohemoglobin. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.18.10378
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
