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

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

Label
A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry
Title
A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry
Creator
Subject
Language
eng
Summary
This book investigates the function and mechanism of a newly discovered heme-thiolate peroxygenase, AaeAPO. Featuring clear illustrations with original research data, it demonstrates that the peroxygenase catalyzes a wide range of reactions
Member of
Cataloging source
MiAaPQ
Literary form
non fiction
Nature of contents
dictionaries
Series statement
Springer Theses Ser
A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry
Label
A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry
Link
http://libproxy.rpi.edu/login?url=https://ebookcentral.proquest.com/lib/rpi/detail.action?docID=4178146
Publication
Copyright
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Carrier category
online resource
Carrier category code
cr
Carrier MARC source
rdacarrier
Color
multicolored
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Contents
  • Parts of this thesis have been published in the following journal articles: -- Supervisor's Foreword -- Abstract -- Acknowledgements -- Contents -- List of Figures -- List of Tables -- List of Schemes -- 1 Hydrocarbon Oxygenation by Heme-Thiolate Enzymes -- Abstract -- 1.1 Introduction -- 1.1.1 Cytochrome P450S (CYPs) -- 1.1.2 Chloroperoxidase (CPO) -- 1.1.3 P450SP alpha and P450BS beta -- 1.1.4 Aromatic Peroxygenase (AaeAPO) -- 1.2 Mechanistic Investigations of Intermediates in the Catalytic Cycle -- 1.2.1 Compound 0 -- 1.2.2 Compound I -- 1.2.3 Compound II -- 1.2.4 Diagnostic Radical Clocks -- 1.2.5 Kinetic Isotope Effects -- 1.3 Application on the Design of New Biocatalysts with Protein Engineering -- 1.4 Conclusions -- References -- 2 Efficient and Selective Alkane Hydroxylation Reactions Catalyzed by the Fungal Peroxygenase AaeAPO -- Abstract -- 2.1 Introduction -- 2.2 Results and Discussion -- 2.2.1 Hydroxylation of Alkanes with High Efficiency and Selectivity -- 2.2.2 Hydroxylation at Benzyl Position with a High Degree of Stereoselectivity -- 2.2.3 Hydroxylation of Neopentane and Ethane -- 2.2.4 Drug Metabolites -- 2.2.5 Flavin Cofactors and Glucose Oxidase Coenzymes -- 2.2.5.1 Too Much H2O2 Can Kill the Activity of the Enzyme -- 2.2.5.2 Glucose Oxidase Coenzymes Catalytic Cycle -- 2.2.5.3 Flavin Cofactors Catalytic Cycle -- 2.3 Conclusions -- 2.4 Experimental -- References -- 3 Hydrocarbon Hydroxylations Catalyzed by AaeAPO: Evidence of Radical Intermediates and Kinetic Isotope Effects -- Abstract -- 3.1 Introduction -- 3.2 Results and Discussion -- 3.2.1 Radical Clocks -- 3.2.1.1 Bicycloheptane -- 3.2.1.2 Bicyclo[2.1.0]Pentane -- 3.2.1.3 TMCP -- 3.2.2 Kinetic Isotope Effect (KIE) -- 3.2.2.1 N-Hexane-1,1,1,2,2,3,3-D7 -- 3.2.2.2 Methyl Group Stepwise Deuterated Toluenes -- 3.2.2.3 Single Methyl Group Deuterated Xylenes
  • 3.2.2.4 Stereo-Deuterated Ethylbenzene -- 3.3 Conclusions -- 3.4 Experimental -- 3.4.1 Synthesis of Substrates and Authentic Samples -- References -- 4 Detection and Kinetic Characterization of a Highly Reactive Heme-Thiolate Peroxygenase AaeAPO Compound I -- Abstract -- 4.1 Results and Discussion -- 4.1.1 Kinetic Characterization of AaeAPO Binding with Substrates -- 4.1.2 Detection and Generation of AaeAPO-I -- 4.1.3 Kinetic Characterization of AaeAPO-I Towards a Series of Alkanes -- 4.2 Conclusions -- 4.3 Experimental -- References -- 5 Driving Force for Oxygen Atom Transfer by Heme-Thiolate Enzymes -- Abstract -- 5.1 Results and Discussion -- 5.1.1 Kinetic Characterization of Compound I Generation by Hypohalous Acids -- 5.1.2 Kinetic Characterization of Compound I Reaction with Halide Ions -- 5.1.3 Determination the Redox Potential of Compound I and the Nernst Plots -- 5.1.4 Implication of Compound I Redox Properties on C--H Activation -- 5.2 Conclusions -- 5.3 Experimental -- References -- 6 Detection and Characterization of Heme-Thiolate Compound II from AaeAPO Peroxygenase -- Abstract -- 6.1 Introduction -- 6.2 Results and Discussion -- 6.2.1 Direct Reductive Generation of AaeAPO-II from AaeAPO-I with Nitroxyl Radicals -- 6.2.2 Determination of the Ferryl--OH pKa in AaeAPO-II -- 6.2.3 Kinetic Characterization of AaeAPO-II Towards Alkanes and Phenols -- 6.3 Conclusions -- 6.4 Experimental -- References -- 7 Cloning and Expression of AaeAPO from Agrocybe aegerita to E. coli, for Studies of Structure-Function Relationships by Site-Specific Mutagenesis -- Abstract -- 7.1 Results and Discussions -- 7.1.1 Purification of Wild Type AaeAPO from Agrocybe aegerita -- 7.1.2 Construction Plasmids Containing apo Gene for the Over-Expression of AaeAPO in E. coli -- 7.1.3 Comparison of Several Fungal Heme-Thiolate Enzymes
  • 7.1.4 EPR Spectra of Resting Enzymes -- 7.1.5 Alkane Hydroxylation Reactivity and Selectivity -- 7.1.6 Intermediate Generation and Stability -- 7.1.7 Site-Specific Mutagenesis for the Study of Structure-Function Relationships -- 7.2 Conclusions -- 7.3 Experimental -- References
http://library.link/vocab/cover_art
https://contentcafe2.btol.com/ContentCafe/Jacket.aspx?Return=1&Type=S&Value=9783319032368&userID=ebsco-test&password=ebsco-test
Dimensions
unknown
http://library.link/vocab/discovery_link
{'f': 'http://opac.lib.rpi.edu/record=b4384260'}
Extent
1 online resource (153 pages)
Form of item
online
Isbn
9783319032368
Media category
computer
Media MARC source
rdamedia
Media type code
c
Sound
unknown sound
Specific material designation
remote

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