Strong modulation of nitrite reductase activity of cytoglobin by disulfide bond oxidation: Implications for nitric oxide homeostasis
Abstract
Globin-mediated nitric oxide (NO) dioxygenase and nitrite reductase activities have been proposed to serve protective functions within the cell by scavenging or generating NO respectively. Cytoglobin has rapid NO dioxygenase activity, similar to other globins, however, the apparent rates of nitrite reductase activity have been reported as slow or negligible. Here we report that the activity of cytoglobin nitrite reductase activity is strongly dependent on the oxidation state of the two surface-exposed cysteine residues. The formation of an intramolecular disulfide bond between cysteines C38 and C83 enhances the nitrite reductase activity by 50-fold over that of the monomer with free sulfhydryl or 140-fold over that of the dimer with intermolecular disulfide bonds. The NO dioxygenase reactivity of cytoglobin is very rapid with or without disulfide bond, however, binding of the distal histidine following dissociation of the nitrate are affected by the presence or absence of the disulfide bond. The nitrite reductase activity reported here for the monomer with intramolecular disulfide is much higher than of those previously reported for other mammalian globins, suggesting a plausible role for this biochemistry in controlling NO homeostasis the cell under oxidative and ischemic conditions.
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
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.
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?
Most ROS/RNS molecules, despite being long considered toxic, have been shown to exert important signaling functions.
“It is worth indicating that despite being long considered toxic species, most of these molecules have been shown to exert important signaling functions”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [778]
Generation of superoxide and hydrogen peroxide mediates critical processes such as angiogenesis, hypoxic adaptation, and energy homeostasis.
“Indeed, the generation of superoxide and hydrogen peroxide, among others, has been shown to mediate critical processes such as angiogenesis, hypoxic adaptation, and energy homeostasis (96, 249, 291, 720, 778, 825, 960).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [778]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
The citation lists haven’t been fetched yet
References 56 · Cited by 50
- Authors
- Reeder, B. J., & Ukeri, J.
- Affiliations
- University of Essex (GB)
- Corresponding author
- Reeder, Brandon J.
- ORCID
- Reeder, Brandon J.
- Venue
- Nitric Oxide
- Publisher
- Elsevier BV
- Published
- 2018-01
- Volume
- 72
- Pages
- 16-23
- ISSN
- 1089-8603 (ISSN-L)
- OpenAlex
- W2767945729
- Cited by
- 50
- References
- 56
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 1 · 2023: 9 · 2022: 9 · 2021: 4 · 2020: 6 · 2019: 4 · 2018: 11
- FWCI
- 3.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nitric Oxide (publishedVersion)
- PubMed (publishedVersion)
- Open Access at Essex (University of Essex) (acceptedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- cytoglobin, nitrite reductase activity, nitric oxide dioxygenase, disulfide bond oxidation, intramolecular disulfide bond, nitric oxide homeostasis, distal histidine, nitrate binding, oxidative stress, ischemia
- MeSH terms
- Cytoglobin, Cysteine, Disulfides, Heme, Humans, Iron, Nitric Oxide, Nitrite Reductases, Oxidation-Reduction, Oxygenases, Recombinant Proteins, Protein Multimerization
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
