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Article

Regulation of nitrite reductase and lipid binding properties of cytoglobin by surface and distal histidine mutations.

Nitric oxide : biology and chemistry - 1 Aug 2022

Kaliszuk Stefan J, Morgan Natasha I, Ayers Taylor N, Sparacino-Watkins Courtney E, DeMartino Anthony W, Bocian Kaitlin, Ragireddy Venkata, Tong Qin, Tejero Jesús

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 35667547
DOI: 10.1016/j.niox.2022.06.001
PMCID: PMC9283305

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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