1;Preface;62;Contents;83;Contributors;104;Chapter 1: Introduction;144.1;References;175;Chapter 2: Molecular Phylogeny of Heme Peroxidases;195.1;2.1 Systematic Classification of Peroxidases;205.2;2.2 The Peroxidase-Cyclooxygenase Superfamily;215.2.1;2.2.1 Bacterial Members: Peroxicins, Peroxidockerins, Primordial Peroxidases;225.2.2;2.2.2 Bacterial, Fungal, and Animal Cyclooxygenases;245.2.3;2.2.3 Ecdysozoan and Echinozoan Peroxinectins;245.2.4;2.2.4 Ecdysozoan and Deuterostomian Peroxidasins;245.2.5;2.2.5 Chordata Peroxidases;285.3;2.3 The Peroxidase-Catalase Superfamily;295.3.1;2.3.1 Class I: Peroxidases;315.3.1.1;2.3.1.1 Catalase-Peroxidases (KatGs);315.3.1.2;2.3.1.2 Ascorbate Peroxidases, Cytochrome c Peroxidases, and Their Putative Hybrid Types;335.3.2;2.3.2 Class II: Manganese, Lignin Peroxidases, and Versatile Peroxidases;355.3.3;2.3.3 Class III: Plant Secretory Peroxidases;355.4;2.4 Di-Heme Peroxidase Family;385.5;2.5 Dyp-Type Heme Peroxidase Family;385.6;2.6 Haloperoxidase Family;425.7;2.7 Conclusions;445.8;References;446;Chapter 3: Structural and Functional Features of Peroxidases with a Potential as Industrial Biocatalysts;486.1;3.1 General Structural Characteristics of Heme Peroxidases;496.1.1;3.1.1 Superfamily of Plant, Fungal, and Bacterial Peroxidases;496.1.2;3.1.2 Superfamily of Mammalian and Other Animal Peroxidases;506.1.3;3.1.3 Other Heme Peroxidase (super)Families;536.2;3.2 Basidiomycete Peroxidases;546.2.1;3.2.1 White-Rot Fungal Peroxidases: Biotechnological Interest;546.2.2;3.2.2 Evolutionary Relationships of Basidiomycete Peroxidases;556.3;3.3 Ligninolytic Peroxidases;576.3.1;3.3.1 Heme Environment;586.3.2;3.3.2 Manganese Oxidation Site;586.3.3;3.3.3 LRET Substrate Oxidation at an Exposed Tryptophan;606.3.4;3.3.4 Influence of the Catalytic Tryptophan Environment;616.4;3.4 Heme-Thiolate Peroxidases;626.4.1;3.4.1 Heme Environment;636.4.2;3.4.2 Substrate Oxidation Sites;646.5;3.5 Dye-Decolorizing Peroxidases;646.6;3.6 Conclusions;656.7;References;667;Chapter 4: Redox Potential of Peroxidases;717.1;4.1 Introduction;717.2;4.2 Redox Potential of the Fe(III)/Fe(II) Couple in Heme Proteins;727.2.1;4.2.1 Thermodynamics of Ferric Heme Reduction;727.2.2;4.2.2 Influence of the Primary Coordination Sphere on Redox Potential;747.2.3;4.2.3 Influence of the Protein Matrix on Redox Potential;757.3;4.3 Redox Potential of Heme Peroxidases;767.3.1;4.3.1 Redox Potential of the Catalytic Species;777.3.2;4.3.2 Modulation of Redox Potential;787.4;4.4 Methods to Measure or Estimate Redox Potential of Heme Peroxidases;817.5;4.5 Conclusions;827.6;References;838;Chapter 5: Catalytic Mechanisms of Heme Peroxidases;888.1;5.1 Introduction;898.2;5.2 Peroxidase Catalytic Cycle;898.2.1;5.2.1 Ferric Peroxidase;918.2.2;5.2.2 Compound 0;928.2.3;5.2.3 Compound I: Porphyrin Radical;928.2.4;5.2.4 Compound I: Protein Radical;938.2.5;5.2.5 Compound II;948.2.6;5.2.6 Compound III;948.3;5.3 Self-Processing of Peroxidases;958.3.1;5.3.1 Protein Modifications;958.3.2;5.3.2 Heme-Protein Crosslinking;978.3.3;5.3.3 Heme Modification by Metabolites;988.4;5.4 Substrate Oxidations;1028.4.1;5.4.1 Oxidative Properties;1028.4.2;5.4.2 One-Electron Oxidations;1038.4.2.1;5.4.2.1 Phenols;1038.4.2.2;5.4.2.2 Aromatic Amines;1058.4.2.3;5.4.2.3 Carbon Oxidation;1068.4.2.4;5.4.2.4 Electron Transfer Relay;1068.4.3;5.4.3 Two-Electron Oxidations;1078.4.3.1;5.4.3.1 Halogenation;1078.4.3.2;5.4.3.2 Oxygen Transfer;1098.4.3.3;5.4.3.3 Sequential One-Electron Oxidations;1098.5;5.5 Conclusions;1108.6;References;1119;Chapter 6: Potential Applications of Peroxidases in the Fine Chemical Industries;1189.1;6.1 Selective Oxidations Catalyzed by Peroxidases;1189.1.1;6.1.1 Introduction;1189.1.2;6.1.2 Reactions Driven by Radical Mechanisms;1219.1.2.1;6.1.2.1 Oxidation of Phenols (oxidative dehydrogenation of phenols);1229.1.2.2;6.1.2.2 Oxidation of Amines;1279.1.2.3;6.1.2.3 Oxidation of Catechols;1289