A distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin.

ABSTRACT: Hydrogen sulfide is a critical signaling molecule, but high concentrations cause cellular toxicity. A four-enzyme pathway in the mitochondrion detoxifies H₂S by converting it to thiosulfate and sulfate. Recent studies have shown that globins like hemoglobin and myoglobin can also oxidize H₂S to thiosulfate and hydropolysulfides. Neuroglobin, a globin enriched in the brain, was reported to bind H₂S tightly and was postulated to play a role in modulating neuronal sensitivity to H₂S in conditions such as stroke. However, the H₂S reactivity of the coordinately saturated heme in neuroglobin is expected a priori to be substantially lower than that of the 5-coordinate hemes present in myoglobin and hemoglobin. To resolve this discrepan

SUBMITTER: Ruetz M 

PROVIDER: S-EPMC5399104 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature