Tuning Heme Functionality: The Cases of Cytochrome c Oxidase and Myoglobin Oxidation
Date Issued
2012
DOI
10.1007/978-3-642-31125-3_24
Abstract
The (Fe-O) moiety of Cytochrome c oxidase ferryl intermediate of
the dioxygen activation reaction and the oxy-myoglobin (Mb-O2) structure have
been probed by QM/MM (hybrid quantum mechanical/ molecular mechanical)
calculations using Density Functional Theory (DFT)/MM to elucidate the effect
of the heme propionates and the protein matrix on the chemistry of heme Fe-O
moieties. On this line, we have probed the role of His97 in various protonation
states of the heme propionate-6 in Mb and compared the results to that of the
Cytochrome c oxidase chemistry.
the dioxygen activation reaction and the oxy-myoglobin (Mb-O2) structure have
been probed by QM/MM (hybrid quantum mechanical/ molecular mechanical)
calculations using Density Functional Theory (DFT)/MM to elucidate the effect
of the heme propionates and the protein matrix on the chemistry of heme Fe-O
moieties. On this line, we have probed the role of His97 in various protonation
states of the heme propionate-6 in Mb and compared the results to that of the
Cytochrome c oxidase chemistry.