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

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

SUBMITTER: Kaliszuk SJ 

PROVIDER: S-EPMC9283305 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature