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Driving Force for Oxygen Atom Transfer by Heme-Thiolate EnzymesOpen image in new window

  • Xiaoshi WangEmail author
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Part of the Springer Theses book series (Springer Theses)

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.

Keywords

Redox Potential Oxygen Atom Transfer Ferric Protein Ferric Enzyme Agrocybe Aegerita 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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© Springer International Publishing Switzerland 2016

Authors and Affiliations

  1. 1.PhiladelphiaUSA

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