Sulfite Oxidase Catalyzes Single-Electron Transfer at Molybdenum Domain to Reduce Nitrite to Nitric Oxide
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Aims: Recent studies suggest that the molybdenum enzymes xanthine oxidase, aldehyde oxidase, and mARC exhibit nitrite reductase activity at low oxygen pressures. However, inhibition studies of xanthine oxidase in humans have failed to block nitrite-dependent changes in blood flow, leading to continued exploration for other candidate nitrite reductases. Another physiologically important molybdenum enzyme—sulfite oxidase (SO)—has not been extensively studied. Results: Using gas-phase nitric oxide (NO) detection and physiological concentrations of nitrite, SO functions as nitrite reductase in the presence of a one-electron donor, exhibiting redox coupling of substrate oxidation and nitrite reduction to form NO. With sulfite, the physiological substrate, SO only facilitates one turnover of nitrite reduction. Studies with recombinant heme and molybdenum domains of SO indicate that nitrite reduction occurs at the molybdenum center via coupled oxidation of Mo(IV) to Mo(V). Reaction rates of nitrite to NO decreased in the presence of a functional heme domain, mediated by steric and redox effects of this domain. Using knockdown of all molybdopterin enzymes and SO in fibroblasts isolated from patients with genetic deficiencies of molybdenum cofactor and SO, respectively, SO was found to significantly contribute to hypoxic nitrite signaling as demonstrated by activation of the canonical NO-sGC-cGMP pathway. Innovation: Nitrite binds to and is reduced at the molybdenum site of mammalian SO, which may be allosterically regulated by heme and molybdenum domain interactions, and contributes to the mammalian nitrate-nitrite-NO signaling pathway in human fibroblasts. Conclusion: SO is a putative mammalian nitrite reductase, catalyzing nitrite reduction at the Mo(IV) center. Antioxid. Redox Signal. 23, 283–294.
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Acute supplementation of BH4, either orally or injected, generally improves vasodilatation.
“Acute supplementation of BH4, either orally or injected, generally improves vasodilatation.”
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Acute BH4 improves vasodilatation in healthy individuals and patients with hypertension, hypercholesterolemia, chronic heart failure, coronary artery disease, heart failure with reduced ejection fraction, rheumatoid arthritis, or smokers.
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- Authors
- Wang, J., Krizowski, S., Fischer-Schrader, K., Niks, D., Tejero, J., Sparacino-Watkins, C., Wang, L., Ragireddy, V., Frizzell, S., Kelley, E. E., Zhang, Y., Basu, P., Hille, R., Schwarz, G., & Gladwin, M. T.
- Affiliations
- University of Pittsburgh (US)
- University of Cologne (DE)
- University of California, Riverside (US)
- Duquesne University (US)
- Cologne University
- Corresponding author
- Gladwin, Mark T.
- ORCID
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2015-08
- Volume
- 23
- Issue
- 4
- Pages
- 283-294
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- PMC
- PMC4523048
- OpenAlex
- W1480282176
- Cited by
- 84
- References
- 52
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 2 · 2023: 12 · 2022: 6 · 2021: 2 · 2020: 9 · 2019: 8 · 2018: 9 · 2017: 8 · 2016: 5 · 2015: 8 · 2014: 3 · 2013: 1
- FWCI
- 2.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Antioxidants and Redox Signaling (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- University of Pittsburgh
- Hemophilia Center of Western Pennsylvania
- Deutsche Forschungsgemeinschaft
- National Institutes of Health (PO1-HL-103455)
- Medical Center, University of Pittsburgh
- National Heart, Lung, and Blood Institute (R01HL096973, P01HL103455, T32HL007563, R01HL098032)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Health Sciences › Medicine › Physiology › Nitric Oxide and Endothelin Effects
- Keywords
- sulfite oxidase, nitrite reductase, nitric oxide production, molybdenum enzymes, single electron transfer, nitrate-nitrite-NO pathway, molybdenum cofactor deficiency, fibroblasts
- MeSH terms
- Molybdenum Cofactors, Coenzymes, Electron Transport, Fibroblasts, Heme, Humans, Metalloproteins, Molybdenum, Nitric Oxide, Nitrites, Oxidation-Reduction, Pteridines, Signal Transduction, Protein Structure, Tertiary, Sulfite Oxidase
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