Abstract
The non-native oxidation of horse heart myoglobin with hydrogen peroxide produces compound II which autoreduces by utilizing an internal oxidation site. Here, we utilize full UV–visible time-dependent kinetics with global kinetic singular value decomposition analysis to explore the mechanism and uncover more detail about the high-valent heme spectral features. By varying the hydrogen peroxide and myoglobin concentration, we were able to uncover more detailed spectra of myoglobin compound II and the autoreduction rate under several different pH conditions. The compound II spectra demonstrate pH-dependent features with an inflection point around pH 5.7 ± 0.1. The rate of autoreduction of compound II, k2, increases with lower pH with a half-power proton dependence and no indication of a pKa > 3.9 ± 0.2, indicating that the autoreduction is still dependent on the protonation of the ferryl oxo species. The k2 also demonstrates both hydrogen peroxide and myoglobin dependency. At myoglobin concentrations greater than 6.6 μM, the k2 is myoglobin-independent, but for lower concentrations, a pH-sensitive concentration dependence is seen.
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