Heme peroxidases / edited by Emma Raven and Brian Dunford.

Format:

Book

Author/Creator:

Emma Raven

Contributor:

Raven, Emma, editor.

Dunford, H. Brian, editor.

Royal Society of Chemistry (Great Britain), issuing body.

Series:

RSC metallobiology series ; 4.

RSC Metallobiology Series, 2045-547X ; 4

Language:

English

Subjects (All):

Peroxidase.

Physical Description:

1 online resource (389 p.)

Place of Publication:

Cambridge, England : Royal Society of Chemistry, 2016.

Language Note:

English

Summary:

This book will provide an up to date handbook that is unique in its combination of both the general aspects of heme protein structure and the function in a single volume.

Contents:

Cover; Contents; Preface; References; Author Biographies; Section 1 Structure and Reactivity of Heme Peroxidases; Chapter 1 Self-processing of Peroxidases; 1.1 Introduction; 1.2 Protein Modifications; 1.2.1 Lignin Peroxidases; 1.2.2 KatG Peroxidases; 1.3 Heme-Protein Crosslinking; 1.3.1 Mammalian Peroxidase Ester Links; 1.3.2 Bacterial Peroxidase Ester Links; 1.3.3 MPO Methionine-Vinyl Crosslink; 1.3.4 Model Reactions; 1.3.5 Role of Methionine-Vinyl Crosslink; 1.3.6 Role of Ester Crosslinks; 1.4 Conclusions; References; Chapter 2 Cytochrome c Peroxidase-Cytochrome c Complexes

2.1 Initial Studies2.2 CCP-cytc Structure; 2.3 One Site or Two?; 2.4 Electron Transfer; 2.5 The CCP Trp Radical; 2.6 Other CCPs; 2.7 LmP-cytc Crystal Structure; 2.8 Summary and Conclusion; References; Chapter 3 Understanding the Reactivity and Interactions of Peroxidases with Substrates; 3.1 Introduction and Early Studies; 3.2 Development of a Framework for Substrate Binding across the Peroxidase Family; 3.3 Binding of Mn(ii) to Peroxidases; 3.4 Binding of Ascorbate to Peroxidases; 3.5 Binding of Hydroxamic Acids to Peroxidases; 3.6 Binding of Isoniazid to Peroxidases

3.7 Binding of Guaiacol and Other Phenolic Substrates to Peroxidases3.8 Summary; References; Chapter 4 Structural and Functional Properties of Heme-containing Peroxidases: a Resonance Raman Perspective for the Superfamily of Plant, Fungal and Bacterial Peroxidases; 4.1 Introduction; 4.2 Superfamily of Plant, Fungal and Bacterial Peroxidases; 4.3 An Overview of the Resonance Raman Spectroscopy of Heme Proteins; 4.3.1 Coordination and Spin States of Heme Proteins; 4.4 Distal Fe-Ligand Modes as a Probe of Heme Cavity Structure; 4.4.1 The Hydroxo Ligand; 4.4.2 The Fluoride Ligand

4.4.3 The CO Ligand4.5 The Proximal Iron-Histidine Stretching Mode: a Sensitive Probe of Proximal Properties; 4.5.1 Status of the Fe-proximal Histidine Bond in Peroxidases; 4.6 Effect of Mutation; 4.6.1 Proximal Mutation-induced Effects in the Distal Cavity; 4.6.2 Distal Mutation-induced Effects in the Proximal Cavity; 4.6.3 Control of Water Binding by Distal Mutation; 4.7 Raman Microscopy Combined with X-ray Crystallography; 4.8 Conclusions; Acknowledgments; References; Chapter 5 Heme Peroxidase Kinetics; 5.1 Introduction; 5.2 Kinetics: from the Steady State to Transient State

5.3 Oxidation States Six to Two5.4 Mechanism of Compound I Formation; 5.5 Neutron Diffraction Experiments on Yeast Cytochrome c Peroxidase; 5.6 Mechanism of Compound I Reduction; 5.6.1 Two-electron Reductions of Compound I; 5.7 Mechanism of Compound II Reduction; 5.8 Steady State Reactions; References; Chapter 6 Multiheme Peroxidases; 6.1 Biological Significance; 6.2 Structural Information; 6.2.1 Architecture of Bacterial Diheme Peroxidases; 6.2.2 Redox-dependent Structural Changes in bCCPs; 6.3 The Mechanism of Peroxide Reduction; 6.3.1 Reductive Activation of the Enzyme

6.3.2 Interaction with the Physiological Electron Donor

Notes:

Description based upon print version of record.

Includes bibliographical references at the end of each chapters and index.

Description based on online resource; title from PDF title page (ebrary, viewed December 10, 2015).

ISBN:

9781782622628

1782622624