Biochimica et Biophysica Acta (BBA) - General Subjects
Mössbauer spectroscopic study of compound es of cytochrome c peroxidase
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Cited by (67)
Cytochrome P450 enzyme mechanisms
2021, Comprehensive Coordination Chemistry IIITryptophan tryptophylquinone biosynthesis: A radical approach to posttranslational modification
2012, Biochimica et Biophysica Acta - Proteins and ProteomicsCitation Excerpt :Another form of the high-valent Fe species in heme proteins is Compound ES (cpd ES), which is composed of an Fe(IV)=O heme and amino acid-based cation radical in close proximity to the high-valent heme. The compound ES description is based on the initial characterization from cytochrome c peroxidase [27]. In cytochrome c peroxidase, the cation radical is found at a Trp residue rather than at the porphyrin.
Enzyme reactivation by hydrogen peroxide in heme-based tryptophan dioxygenase
2011, Journal of Biological ChemistryCitation Excerpt :At approximately the same reaction time as the Mössbauer sample, the spin concentration of the protein radical is found to be comparable with the concentration of the Fe(IV)=O heme species. Together, these results suggest the formation of an intermediate composed of an Fe(IV)=O heme in close proximity to the free radical, similar to the so-called compound ES description based on the initial characterization from cytochrome c peroxidase (37, 38). Compound ES of cytochrome c peroxidase is a semi-stable enzyme intermediate that contains an Fe(IV)=O heme and a Trp radical (39).
The mystery of cytochrome P450 Compound I: A mini-review dedicated to Klaus Ruckpaul
2011, Biochimica et Biophysica Acta - Proteins and ProteomicsThirty years of heme peroxidase structural biology
2010, Archives of Biochemistry and BiophysicsCitation Excerpt :The term “oxene” intermediate was adopted [19] in honor of the similarly reactive and better understood carbene. It was also known from magnetic susceptibility studies [20] and Mossbauer [21] that the redox state of the iron is Fe(IV). Taken together these data coupled with the finding that peroxidases and catalases form π cation radicals in Compound I [22], consistent with model heme studies [23], meant that the oxene O atom left behind after heterolysis of the OO bond removes one electron from the iron and one from the porphyrin.
On the status of ferryl protonation
2006, Journal of Inorganic Biochemistry