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A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry

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  • © 2016
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Overview

Authors:
  1. Xiaoshi Wang

    1. Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, USA

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  • Nominated as an outstanding Ph.D. thesis by Princeton University, USA
  • Represents significant scientific advance in the field of heme-thiolate enzymes
  • Provides clear and colorful illustrations with original research data
  • Give complete and detailed enzymatic function studies and mechanistic frameworks
  • Includes supplementary material: sn.pub/extras

Part of the book series: Springer Theses (Springer Theses)

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Table of contents (7 chapters)

  1. Front Matter

    Pages i-xxxii
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  2. Hydrocarbon Oxygenation by Heme-Thiolate Enzymes

    • Xiaoshi Wang
    Pages 1-21
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  3. Efficient and Selective Alkane Hydroxylation Reactions Catalyzed by the Fungal Peroxygenase AaeAPO

    • Xiaoshi Wang
    Pages 23-40
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  4. Hydrocarbon Hydroxylations Catalyzed by AaeAPO: Evidence of Radical Intermediates and Kinetic Isotope Effects

    • Xiaoshi Wang
    Pages 41-57
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  5. Detection and Kinetic Characterization of a Highly Reactive Heme-Thiolate Peroxygenase AaeAPO Compound I

    • Xiaoshi Wang
    Pages 59-74
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  6. Driving Force for Oxygen Atom Transfer by Heme-Thiolate Enzymes

    • Xiaoshi Wang
    Pages 75-89
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  7. Detection and Characterization of Heme-Thiolate Compound II from AaeAPO Peroxygenase

    • Xiaoshi Wang
    Pages 91-111
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  8. Cloning and Expression of AaeAPO from Agrocybe aegerita to E. coli, for Studies of Structure-Function Relationships by Site-Specific Mutagenesis

    • Xiaoshi Wang
    Pages 113-130
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Keywords

About this book

In this thesis, Xiaoshi Wang investigates the function and mechanism of a newly discovered heme-thiolate peroxygenase, AaeAPO. This enzyme class comes from Agrocybe aegerita and is used in the conversion of inert hydrocarbons to alcohols. Xiaoshi's work focuses on an extracellular P450 enzyme which is not limited in its stability and lack of solubility and therefore is relevant for widespread industrial use. The author demonstrates that the peroxygenase catalyzes a wide range of reactions. In some cases the author even describes very difficult transformations in molecules that are highly inert. Her detailed investigations provide a mechanistic framework for how the peroxygenase catalyzes such a large number of reactions. A major highlight of this thesis is the identification of key short-lived intermediates in the catalytic cycle of the peroxygenase, using rapid kinetic and spectroscopic methods, as well as the elucidation of the thermodynamic properties of these high-energy intermediates. This work adds new insight into an important class of enzymes.

Authors and Affiliations

  • Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, USA

    Xiaoshi Wang

About the author

Xiaoshi Wang received her B.Sc. in chemistry from Nanjing University, China in 2007. She obtained her Ph.D. in chemistry from Chemistry Department of Princeton University in August 2013. Her major research project in Prof. John T. Groves group is function and mechanistic investigation on C-H oxygenation reactions catalyzed by heme-thiolate enzymes. Subsequently, she became a post-doc fellow working with Prof. Benjamin Garcia at Perelman School of Medicine, University of Pennsylvania, focusing on studying chromatin protein PTMs during epigenetic processes.

Bibliographic Information

  • Book Title: A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry

  • Authors: Xiaoshi Wang

  • Series Title: Springer Theses

  • DOI: https://doi.org/10.1007/978-3-319-03236-8

  • Publisher: Springer Cham

  • eBook Packages: Chemistry and Materials Science, Chemistry and Material Science (R0)

  • Copyright Information: Springer International Publishing Switzerland 2016

  • Hardcover ISBN: 978-3-319-03235-1Published: 26 October 2015

  • Softcover ISBN: 978-3-319-35428-6Published: 23 August 2016

  • eBook ISBN: 978-3-319-03236-8Published: 16 October 2015

  • Series ISSN: 2190-5053

  • Series E-ISSN: 2190-5061

  • Edition Number: 1

  • Number of Pages: XXXII, 130

  • Topics: Organic Chemistry, Enzymology, Catalysis

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