ArticleNitric oxide : biology and chemistry2022
Regulation of nitrite reductase and lipid binding properties of cytoglobin by surface and distal histidine mutations.
Article in Nitric oxide : biology and chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Cytochrome bFree radical biology & medicine · 2026Article
- CytochromebioRxiv : the preprint server for biology · 2025Article
- Myoglobin inhibits breast cancer cell fatty acid oxidation and migration via heme-dependent oxidant production and not fatty acid binding.Free radical biology & medicine · 2024Article
- Gas-sensing riboceptors.RNA biology · 2024Article
- Engineering neuroglobin nitrite reductase activity based on myoglobin models.Biochemistry and biophysics reports · 2023Article
- Insights into the function of cytoglobin.Biochemical Society transactions · 2023Review
- Modulating Nitric Oxide Dioxygenase and Nitrite Reductase of Cytoglobin through Point Mutations.Antioxidants (Basel, Switzerland) · 2022Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Cytoglobin is a hemoprotein widely expressed in fibroblasts and related cell lineages with yet undefined physiological function. Cytoglobin, as other heme proteins, can reduce nitrite to nitric oxide (NO) providing a route to generate NO in vivo in low oxygen conditions. In addition, cytoglobin can also bind lipids such as oleic acid and cardiolipin with high affinity. These two processes are potentially relevant to cytoglobin function. Little is known about how specific amino acids contribute to nitrite reduction and lipid binding. Here we investigate the role of the distal histidine His81 (E7) and several surface residues on the regulation of nitrite reduction and lipid binding. We observe that the replacement of His81 (E7) greatly increases heme reactivity towards nitrite, with nitrite reduction rate constants of up to 1100 M
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