| Literature DB >> 3191138 |
A C Shosheva1, P K Christova, B P Atanasov.
Abstract
The electron transfer between the excited triplet state of zinc-substituted sperm whale myoglobin and Cu2+ has been studied by following the decay rate of delayed fluorescence. The Cu2+ bound on the surface of the myoglobin molecule are efficient quenchers of the excited electron state of Zn-myoglobin. Two bimolecular rate constants of quenching (KQ) for every pH investigated have been calculated. The pH-dependence of KQ1 indicates that the protonation of one amino acid residue (His-GH1 (119] is important for the process. Our results support the idea of the common nature of the mechanism of quenching by Cu2+ and oxidation of oxymyoglobin by Cu2+.Entities:
Mesh:
Substances:
Year: 1988 PMID: 3191138 DOI: 10.1016/0167-4838(88)90273-7
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002