Dioxygen-dependent Heme Enzymes (eBook, PDF)

Redaktion: Ikeda-Saito, Masao; Raven, Emma

• Format: PDF

Produktbeschreibung

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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Produktdetails

• Verlag: Royal Society of Chemistry
• Seitenzahl: 376
• Erscheinungstermin: 1. Oktober 2018
• Englisch
• ISBN-13: 9781788012911
• Artikelnr.: 54539727

Inhaltsangabe

Dioxygen Binding and Activation Mediated by Transition Metal Porphyrinoid
Complexes; Design and Engineering
of 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 MauG;
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