Towards understanding non-equivalence of α and β subunits within human hemoglobin in conformational relaxation and molecular oxygen rebinding.

ABSTRACT: Picosecond to millisecond laser time-resolved transient absorption spectroscopy was used to study molecular oxygen (O₂) rebinding and conformational relaxation following O₂ photodissociation in the α and β subunits within human hemoglobin in the quaternary R-like structure. Oxy-cyanomet valency hybrids, α₂(Fe²⁺-O₂)β₂(Fe³⁺-CN) and α₂(Fe³⁺-CN)β₂(Fe²⁺-O₂), were used as models for oxygenated R-state hemoglobin. An extended kinetic model for geminate O₂ rebinding in the ferrous hemoglobin subunits, ligand migration between the primary and secondary docking site(s), and nonexponential tertiary relaxation within the R quaternary structure, was introduced a

SUBMITTER: Lepeshkevich SV 

PROVIDER: S-EPMC8153241 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature