ArticleThe Journal of biological chemistry2010
Nitric-oxide dioxygenase function of human cytoglobin with cellular reductants and in rat hepatocytes.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 95 citations in OpenAlex.
- Cytochrome bFree radical biology & medicine · 2026Article
- CytochromebioRxiv : the preprint server for biology · 2025Article
- Neuroglobin and Cytoglobin in Mammalian Nervous Systems: About Distribution, Regulation, Function, and Some Open Questions.Brain sciences · 2025Review
- The cytoglobin-dependent transcriptome in melanoma indicates a protective function associated with oxidative stress, inflammation and cancer-associated pathways.Scientific reports · 2024Article
- Cytoglobin regulates NO-dependent cilia motility and organ laterality during development.Nature communications · 2023Article
- Insights into the function of cytoglobin.Biochemical Society transactions · 2023Review
- Neuronal Cytoglobin in the Auditory Brainstem of Rat and Mouse: Distribution, Cochlear Projection, and Nitric Oxide Production.Brain sciences · 2023Article
- Ordered Motions in the Nitric-Oxide Dioxygenase Mechanism of Flavohemoglobin and Assorted Globins with Tightly Coupled Reductases.Advances in experimental medicine and biology · 2023Article
- Modulating Nitric Oxide Dioxygenase and Nitrite Reductase of Cytoglobin through Point Mutations.Antioxidants (Basel, Switzerland) · 2022Article
- Regulation of nitrite reductase and lipid binding properties of cytoglobin by surface and distal histidine mutations.Nitric oxide : biology and chemistry · 2022Article
- Modulating the Antioxidant Response for Better Oxidative Stress-Inducing Therapies: How to Take Advantage of Two Sides of the Same Medal?Biomedicines · 2022Review
- Role of cytoglobin in cigarette smoke constituent-induced loss of nitric oxide bioavailability in vascular smooth muscle cells.Nitric oxide : biology and chemistry · 2022Article
- Redox-Regulation of α-Globin in Vascular Physiology.Antioxidants (Basel, Switzerland) · 2022Article
- Cytoglobin has potent superoxide dismutase function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Bioinformatics analysis of differentially expressed proteins in alcoholic fatty liver disease treated with recombinant human cytoglobin.Molecular medicine reports · 2021Article
- Cytoglobin protects cancer cells from apoptosis by regulation of mitochondrial cardiolipin.Scientific reports · 2021Article
- Spatially Targeted Proteomics of the Host-Pathogen Interface during Staphylococcal Abscess Formation.ACS infectious diseases · 2021Article
- Redox sensor properties of human cytoglobin allosterically regulate heme pocket reactivity.Free radical biology & medicine · 2021Article
- Role of cytoglobin, a novel radical scavenger, in stellate cell activation and hepatic fibrosis.Clinical and molecular hepatology · 2020Review
- Regulation of Nitric Oxide Metabolism and Vascular Tone by Cytoglobin.Antioxidants & redox signaling · 2020Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Cytoglobin (Cygb) was investigated for its capacity to function as a NO dioxygenase (NOD) in vitro and in hepatocytes. Ascorbate and cytochrome b(5) were found to support a high NOD activity. Cygb-NOD activity shows respective K(m) values for ascorbate, cytochrome b(5), NO, and O(2) of 0.25 mm, 0.3 microm, 40 nm, and approximately 20 microm and achieves a k(cat) of 0.5 s(-1). Ascorbate and cytochrome b(5) reduce the oxidized Cygb-NOD intermediate with apparent second order rate constants of 1000 m(-1) s(-1) and 3 x 10(6) m(-1) s(-1), respectively. In rat hepatocytes engineered to express human Cygb, Cygb-NOD activity shows a similar k(cat) of 1.2 s(-1), a K(m)(NO) of 40 nm, and a k(cat)/K(m)(NO) (k'(NOD)) value of 3 x 10(7) m(-1) s(-1), demonstrating the efficiency of catalysis. NO inhibits the activity at [NO]/[O(2)] ratios >1:500 and limits catalytic turnover. The activity is competitively inhibited by CO, is slowly inactivated by cyanide, and is distinct from the microsomal NOD activity. Cygb-NOD provides protection to the NO-sensitive aconitase. The results define the NOD function of Cygb and demonstrate roles for ascorbate and cytochrome b(5) as reductants.
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