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A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry pp 75–89Cite as

Driving Force for Oxygen Atom Transfer by Heme-Thiolate Enzymes

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Abstract

The heme-thiolate peroxygenase AaeAPO from Agrocybe aegerita is an important biocatalyst and P450 analog. We have found that AaeAPO compound I can be formed via oxidation of the ferric protein with HOBr and HOCl. The rate constant for the formation of AaeAPO-I induced by HOBr at pH 5.0, 4 °C was 7.1 × 10 M−1s−1. AaeAPO-I reacts with bromide and chloride ions to regenerate the resting ferric protein. Similar measurements were made for chloroperoxidase (CPO). The rate constant for the reaction of AaeAPO-I with bromide ion at pH 5.0, 4 °C was 2.6 × 105 M−1s−1. By measuring the rates of the forward and reverse reactions over a wide range of pH, Nernst plots of the driving force for oxygen atom transfer from AaeAPO-I and CPO-I can be constructed. It is found that CPO-I and AaeAPO-I have a two-electron redox potential similar to that of HOBr and about 200 mV less than that of HOCl. Interestingly, CPO-I and AaeAPO-I are both much more oxidizing than HRP compound I. The results are informative with regard to the reactivity of these proteins toward C–H bonds.

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    Xiaoshi Wang

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Wang, X. (2016). Driving Force for Oxygen Atom Transfer by Heme-Thiolate Enzymes . In: A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-03236-8_5

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