Covers the vastly expanding subject of oxidative processes
mediated by copper ions within biological systems
Copper-mediated biological oxidations offer a broad range of
fundamentally important and potentially practical chemical
processes that cross many chemical and pharmaceutical disciplines.
This newest volume in the Wiley Series on Reactive
Intermediates in Chemistry and Biology is divided into three
logical areas within the topic of copper/oxygen chemistry–
biological systems, theory, and bioinorganic models and
applications–to explore the biosphere for its highly evolved
and thus efficient oxidative transformations in the discovery of
new types of interactions between molecular oxygen and copper ion.
Featuring a diverse collection of subject matter unified in one
complete and comprehensive resource, Copper-Oxygen Chemistry probes
the fundamental aspects of copper coordination chemistry, synthetic
organic chemistry, and biological chemistry to reveal both the
biological and chemical aspects driving the current exciting
research efforts behind copper-oxygen chemistry. In addition,
Copper-Oxygen Chemistry:
* Addresses the significantly increasing literature on oxygen-atom
insertion and carbon-carbon bond-forming reactions as well as
enantioselective oxidation chemistries
* Progresses from biological systems to spectroscopy and theory,
and onward to bioinorganic models and applications
* Covers a wide array of reaction types such as insertion and
dehydrogenation reactions that utilize the cheap, abundant, and
energy-containing O2 molecule
With thorough coverage by prominent authors and researchers
shaping innovations in this growing field, this valuable reference
is essential reading for bioinorganic chemists, as well as organic,
synthetic, and pharmaceutical chemists in academia and
industry.
Mục lục
Preface to Series vii
Introduction ix
Contributors xi
1 Insights into the Proposed Copper-Oxygen Intermediates
that Regulate the Mechanism of Reactions Catalyzed by Dopamine
b-Monooxygenase, Peptidylglycine a-Hydroxylating Monooxygenase, and
Tyramine b-Monooxygenase 1
Robert L. Osborne and Judith P. Klinman
2 Copper Dioxygenases 23
Jozsef Kaizer, Jozsef Sandor Pap, and Gabor Speier
3 Amine Oxidase and Galactose Oxidase 53
Dalia Rokhsana, Eric M. Shepard, Doreen E. Brown, and David M.
Dooley
4 Energy Conversion and Conservation by Cytochrome Oxidases
107
Angela Paulus and Simon de Vries
5 Multicopper Proteins 131
Takeshi Sakurai and Kunishige Kataoka
6 Structure and Reactivity of Copper-Oxygen Species
Revealed by Competitive Oxygen-18 Isotope Effects 169
Justine P. Roth
7 Theoretical Aspects of Dioxygen Activation in Dicopper Enzymes
197
Kazunari Yoshizawa
8 Chemical Reactivity of Copper Active-Oxygen Complexes
225
Shinobu Itoh
9 Cytochrome c Oxidase and Models 283
Zakaria Halime and Kenneth D. Karlin
10 Supramolecular Copper Dioxygen Chemistry 321
Jean-Noel Rebilly and Olivia Reinaud
11 Organic Synthetic Methods Using Copper Oxygen Chemistry
361
Marisa C. Kozlowski
Index 445
Giới thiệu về tác giả
Kenneth D. Karlin is Ira Remsen Professor of Chemistry at
Johns Hopkins University. His bioinorganic research focuses on
coordination chemistry relevant to biological and environmental
processes, involving copper or heme (porphyrin-iron) complexes. Dr.
Karlin’s main approach involves synthetic modeling, i.e.,
biomimetic chemistry. He is the winner of the prestigious F. Albert
Cotton Award in Synthetic Inorganic Chemistry and the Sierra Nevada
Distinguished Chemist Award, both awarded in 2009.
Shinobu Itoh focuses his current research on chemical
modeling and application of novel active sites in biological
systems. He was formerly an assistant professor at Osaka
University, where he worked on the chemistry of coenzyme PQQ and
cofactor TTQ as well as model compounds of galactose oxidase. In
1994, he was promoted to associate professor at Osaka University,
where he collaborated with Professor Shunichi Fukuzumi in
copper-dioxygen chemistry research. In 1999, he moved to Osaka City
University as a full professor and started biological studies of
dinuclear copper proteins, such as hemocyanin and tyrosinase. He
returned to Osaka University in 2008 and further expanded his
research interests to the design of artificial non-heme
metalloenzymes using genetic engineering.
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