A reaction pathway to compound 0 intermediates in oxy-myoglobin through interactions with hydrogen sulfide and His64.

ABSTRACT: Myoglobin (Mb) binds oxygen with high affinity as a low spin singlet complex and thus functions as an oxygen storage protein. Yet, hybrid Density Functional Theory/Molecular Mechanical (DFT/MM) calculations of oxy-Mb models predict that the O₂ bond is much less resistant to breaking in the presence of hydrogen sulfide (H₂S) compared with water. Specifically, a hydrogen atom from H₂S can be transferred to the distal oxygen atom through homolytic cleavage of the S-H bond to form the intermediate Compound (Cpd) 0 structure and a thiyl radical. In the presence of a neutral His64 (Nε protonation, His64-ε) and H₂S, only a metastable Cpd 0 would be formed as the active site is devoid of any additional proton donor to fully break the O₂ bond.

SUBMITTER: Rodriguez-Mackenzie AD 

PROVIDER: S-EPMC8256827 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature