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006 m o d
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019 1075623452
020 9781788012911|q(electronic book)
020 1788012917|q(electronic book)
020 |z9781782629917
020 |z1782629912
035 (OCoLC)1057284047|z(OCoLC)1075623452
040 AU@|beng|erda|epn|cAU@|dOCLCO|dUKRSC|dUIU|dOCLCF|dN$T
|dEBLCP|dLVT|dYDX|dMERER|dOCLCQ|dOCLCA|dOCLCQ
049 RIDW
050 4 QP603.H45
072 7 SCI|x007000|2bisacsh
082 04 572/.791|223
090 QP603.H45
245 00 Dioxygen-dependent heme enzymes /|ceditors: Masao Ikeda-
Saito, Emma Raven.
264 1 Cambridge, England :|bRoyal Society of Chemistry,|c2018.
264 4 |c©2019
300 1 online resource :|billustrations.
336 text|btxt|2rdacontent
337 computer|bc|2rdamedia
338 online resource|bcr|2rdacarrier
340 |gpolychrome|2rdacc
347 text file|2rdaft
490 1 Metallobiology Series,|x2045-5488 ;|vno. 13
504 Includes bibliographical references and index.
505 0 Cover; Dioxygen-dependent Heme Enzymes; Preface;
Biographies; Contents; Section I -- Model Systems; Chapter
1 -- Dioxygen Binding and Activation Mediated by
Transition Metal Porphyrinoid Complexes; 1.1 Introduction;
1.2 Role of Transition Metals in Binding and Activating
O2; 1.3 Metalloproteins That Bind and Transport O2; 1.4
Activation of O2 by Heme Enzymes; 1.4.1 Heme
Monooxygenases; 1.4.1.1 Cytochrome P450; 1.4.1.2 Nitric
Oxide Synthase; 1.4.1.3 Heme Oxygenase; 1.4.2 Heme
Dioxygenases; 1.4.2.1 Tryptophan 2,3-Dioxygenase (TDO) and
Indoleamine 2,3-Dioxygenase (IDO)
505 8 1.5 Metallo-porphyrin and -Porphyrinoid Models for O2
Binding and Activation1.5.1 Iron Complexes; 1.5.1.1 Iron
Porphyrins, Phthalocyanines, and Porphyrazines; 1.5.1.2
Iron Corroles and Corrolazines; 1.5.2 Manganese Complexes;
1.5.2.1 Manganese Porphyrins, Phthalocyanines, and
Porphyrazines; 1.5.2.2 Manganese Corroles and
Corrolazines; 1.6 Summary and Future Directions;
Acknowledgements; References; Chapter 2 -- Design and
Engineering of Heme Enzymes With O2-dependent Catalytic
Activity; 2.1 Introduction; 2.2 Structural and Functional
Models of Heme-containing Monooxygenases and Dioxygenases
505 8 2.2.1 The Biological Function of the Cytochrome P450
Monooxygenases2.2.2 The Active Site and Catalytic Cycle of
the Cytochrome P450 Monooxygenases; 2.3 Recent Designs
that Utilize Alanine Scanning; 2.4 Semi-rational and
Rational Design of the P450 Enzymes; 2.5 P450s as a Model
for Dioxygen Activation; 2.6 Heme Dioxygenases; 2.7
Functional Models of the Heme-containing Oxidases; 2.7.1
Biological Functions of Terminal Oxidases; 2.7.2 Structure
of Heme-Copper Oxidases; 2.7.3 Biosynthetic Models of Heme
-Copper Oxidase in Myoglobin; 2.7.3.1 Functional Model of
a Heme-Copper Center in a Mb Scaffold
505 8 2.7.3.2 Fine Tuning the Oxidase Activity with Non-native
Heme Cofactors2.7.3.3 The Role of Non-heme Metal in
Promoting O-O Bond Cleavage; 2.7.3.4 Non-covalent
Interactions in Tuning the Reduction Potential and Proton
Transfer; 2.7.3.5 Defining the Role of the Active Site
Tyrosine by Genetic Incorporation of Tyrosine Analogs;
2.7.3.6 Improving the Oxidase Activity by Optimization of
Interfacial Electron Transfer; 2.7.4 Oxygen Activation by
de novo Designed Heme Proteins; 2.7.4.1 De novo Designed
Heme-binding Maquettes; 2.7.4.2 Oxygen Binding and
Activation by Cytochrome c Maquettes
505 8 2.7.4.3 Heme Oxygenase Activity of Heme-binding
Maquettes2.7.4.4 Electrocatalytic Oxygen Reduction by
Mimochromes; 2.8 Heme-binding DNA/RNAzymes; 2.8.1 Heme-
binding Aptamers with Oxidase Activity; 2.8.2 Scope of
Oxidation Activity by Heme-binding DNA/RNAzymes; 2.9
Conclusions and Future Perspectives; Acknowledgements;
References; Chapter 3 -- Myoglobin Derivatives
Reconstituted with Modified Metal Porphyrinoids as
Structural and Functional Models of the Cytochrome P450
Enzymes; 3.1 Introduction; 3.2 Reconstitution of
Hemoproteins
520 This book highlights the many and varied catalytic
activities of O2-dependent heme-iron enzymes, including
monoxygenases and cytochrome P450, dioxygenases, oxidases
and model heme systems required for postgraduate students
and researchers in biochemistry and metallobiology.
590 eBooks on EBSCOhost|bEBSCO eBook Subscription Academic
Collection - North America
650 0 Heme oxygenase.|0https://id.loc.gov/authorities/subjects/
sh91006132
650 0 Organometallic compounds.|0https://id.loc.gov/authorities/
subjects/sh85095561
650 0 Biochemistry.|0https://id.loc.gov/authorities/subjects/
sh85014171
650 7 Heme oxygenase.|2fast|0https://id.worldcat.org/fast/954951
650 7 Organometallic compounds.|2fast|0https://id.worldcat.org/
fast/1047971
650 7 Biochemistry.|2fast|0https://id.worldcat.org/fast/831961
655 4 Electronic books.
700 1 Ikeda-Saito, Masao,|0https://id.loc.gov/authorities/names/
n2019181891|eeditor.
700 1 Raven, Emma,|eeditor.
776 08 |iPrint version:|tDioxygen-dependent heme enzymes.
|dCambridge, England : Royal Society of Chemistry, 2018
|z9781782629917|z1782629912|w(OCoLC)1035437103
776 08 |iElectronic version:|tDioxygen-dependent heme enzymes.
|dCambridge, England : Royal Society of Chemistry, 2018
|z9781788012911|w(OCoLC)1057284047
830 0 RSC metallobiology series ;|0https://id.loc.gov/
authorities/names/no2014010521|vno. 13.
856 40 |uhttps://rider.idm.oclc.org/login?url=http://
search.ebscohost.com/login.aspx?direct=true&scope=site&
db=nlebk&AN=1939619|zOnline eBook via EBSCO. Access
restricted to current Rider University students, faculty,
and staff.
856 42 |3Instructions for reading/downloading the EBSCO version
of this eBook|uhttp://guides.rider.edu/ebooks/ebsco
901 MARCIVE 20231220
948 |d20200122|cEBSCO|tEBSCOebooksacademic NEW 12-21,1-17
11948|lridw
994 92|bRID
