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Aerobic organisms have evolved to utilise the intrinsic oxidising power of oxygen from the atmosphere. This so-called ‘activation’ of oxygen is often catalysed by a heme-containing enzyme. 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.
Dioxygen-dependent Heme Enzymes will be a useful resource for postgraduate students and researchers in biochemistry and metallobiology working in, or moving into, research areas involving heme proteins.
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Dioxygen Binding and Activation Mediated by Transition Metal Porphyrinoid Complexes; Design and Engineeringof Heme Enzymes With O2-dependent Catalytic Activity; Myoglobin Derivatives Reconstituted with Modified Metal Porphyrinoids as Structural and Functional Models of the Cytochrome P450 Enzymes; Investigating Heme Enzymes with Expanded Genetic Codes; What Drives the Ratedetermining Step for Oxygen Atom Transfer by Heme Compound I?; Cytochrome P450 Decarboxylases; Oxygen Activation and Long-range Electron Transfer in Mau G; Biological Heme Degradation; Structure, Function and Regulation of Human Heme-based Dioxygenases; Modeling O2-dependent Heme Enzymes: A Quick Guide for Non-experts; Structures of Human Cytochrome P450 Enzymes: Variations on a Theme; Controlling the Regio- and Stereoselectivity of Cytochrome P450 Monooxygenases by Protein Engineering; Conformational Changes in Cytochrome P450cam and the Effector Role of Putidaredoxin; Oxygen Reduction and Proton Translocation by Respiratory Cytochrome c Oxidase; Structure and Function of Membrane-bound Bacterial Nitric Oxide Reductases; Mechanisms of Nitric Oxide Sensing and Detoxification by Bacterial Hemoproteins
Bahasa Inggeris ● Format EPUB ● Halaman-halaman 376 ● ISBN 9781788015417 ● Saiz fail 24.4 MB ● Penyunting Masao Ikeda-Saito & Emma Raven ● Penerbit Royal Society of Chemistry ● Diterbitkan 2018 ● Edisi 1 ● Muat turun 24 bulan ● Mata wang EUR ● ID 6723589 ● Salin perlindungan Adobe DRM
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