Handbook on Metalloproteins

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ISBN: 9780824705206 | 0824705203
Cover: Hardcover
Copyright: 6/29/2001

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A collection of 23 chapters combining to provide a tool for the development of biological inorganic chemistry. Aims to provide insights to those not in the field, as well as those in general coordination chemistry, biotechnology, biophysics, medicine, or pharmacology.

Preface

iii

Contributors

xxi

Titles of Related Interest: Handbook on Toxicity of Inorganic Compounds

xxv

Handbook on Metals in Clinical and Analytical Chemistry

xxv

Metal Ions in Biological Systems (list of volumes)

xxv

Color Figures

xxx

Scope and Use of the Handbook

(8)

Ivano Bertini

Astrid Sigel

Helmut Sigel

Scope of the Handbook

(2)

Organization of the Handbook

(1)

Some Web Sites for Further Information

(1)

General Comments and Outlook

(4)

References

(3)

Interaction of Sodium and Potassium with Proteins

(30)

Todd M. Larsen

George H. Reed

Introduction

(1)

Bioinorganic Chemistry of Na+ and K+

(1)

Coordination Chemistry of Na+ and K+

(1)

Enzymes/Proteins with Known Structure

(4)

Enzymes/Proteins with Unknown Structure

(1)

Structure-Function Relationships

(16)

Dialkylglycine Decarboxylase

(1)

Pyruvate Kinase

(3)

Diol Dehydratase

(1)

Hsc70

(2)

Class II Fructose-1,6-Bisphosphate Aldolase

(1)

Fructose-1,6-Bisphosphatase

(1)

Carbamoyl Phosphate Synthetase

(1)

Cytochrome P450cam

(1)

S-Adenosylmethionine Synthetase

(1)

Tryptophan Synthase α2β2 Complex

(1)

Tryptophanase

(2)

Tyrosine Phenol-Lyase

(1)

Ascorbate Peroxidase

(1)

Methionine Aminopeptidase

(1)

Thrombin

(1)

α-Amylase

(1)

Perspectives

(8)

Acknowledgments

(1)

Abbreviations and Definitions

(1)

References

(7)

Structure and Function of Sodium and Potassium Channel Proteins in Membranes

(20)

Bernd Fakler

Introduction

(1)

Ion Channels: Definition and Role in Excitable Membranes

(1)

How Do Voltage-Gated Ion Channels Work?

(1)

Potassium and Sodium Channel Proteins with Known Primary Structure

(4)

Potassium Channels

(2)

Sodium Channels

(1)

Structures of Channel Proteins and Protein Domains Resolved to Date

(3)

The Pore of a Bacterial Potassium Channel

(2)

Inactivation Domains of Mammalian Potassium and Sodium Channels

(1)

Structure-Function Relationships

(5)

Selectivity and Permeation

(2)

Gating: Activation and Inactivation

(3)

Perspectives

(6)

Acknowledgments

(1)

Abbreviations and Definitions

(1)

References

(5)

Magnesium-Activated Enzyme Systems

(34)

Allan Matte

Louis T. J. Delbaere

Introduction

(4)

Chemistry of Magnesium

(1)

Magnesium-Ligand Chemistry

(1)

Metabolism of Magnesium within Prokaryotic and Eukaryotic Cells

(2)

Known Structures in Magnesium-Activated Enzyme Systems

(8)

Bi-Mg2+-Bound Structures

(1)

Kinases

(1)

Mg2+-Induced Conformational Changes in Proteins

(1)

Unknown Structures

(2)

Magnesium-Protoporphyrin IX Chelatase

(1)

Sphingomyelinase

(1)

Mycobacterial GDP-Mannose Pyrophosphorylase

(1)

N1-(5'-Phosphoribosyl)adenosine-5'-monophosphate Cyclohydrolase

(1)

Structure-Function Relationships

(8)

Kinases

(3)

DNA Polymerases

(1)

p21ras

(1)

Ribozymes

(1)

Isocitrate Dehydrogenase

(1)

Xylose Isomerase

(1)

Conclusions

(11)

Acknowledgments

(1)

Abbreviations

(2)

References

(9)

Calcium and Its Enzymes

(60)

Andreas Muranyi

Bryan E. Finn

Introduction

(6)

Aims and Scope

(1)

Coordination Chemistry of Ca2+

(1)

Bioinorganic Role of Ca2+

(1)

Homeostasis and Metabolism

(2)

Distribution of Ca2+-Binding Proteins

(2)

Introduction to Systems Chosen for Discussion

(1)

Enzymes/Proteins with Known Structure

100

(39)

EF-Hand Proteins

100

(15)

Annexins

115

(6)

C2 Domains

121

(7)

EGF-Like Modules

128

(5)

Lectins

133

(6)

Enzymes/Proteins with Unknown Structure

139

(1)

Structure-Function Relationships

140

(1)

Perspectives

140

(1)

Ca2+ and Protein-Related Internet Resources

141

(12)

Abbreviations and Definitions

141

(1)

References

142

(11)

Vanadium in Proteins and Enzymes

153

(28)

Alison Butler

Jayme N. Carter

Matthew T. Simpson

Introduction

154

(1)

Coordination Chemistry of Vanadium

154

(1)

Bioinorganic Role of Vanadium

155

(1)

Vanadium Enzymes with Known Structure: Vanadium Haloperoxidases

155

(12)

Vanadium Chloroperoxidase

157

(8)

Vanadium Bromoperoxidase

165

(2)

Vanadium Enzymes of Unknown Structure: Vanadium Nitrogenase

167

(2)

Occurrence and Biological Significance

167

(1)

Structural Considerations and Reactivity

168

(1)

Structure-Function Relationships

169

(4)

Vanadium Haloperoxidase Expression Systems

169

(1)

Comparative Aspects of the Vanadium Sites in V-BrPO and V-CIPO

170

(2)

Mechanistic Considerations of the Catalytic Cycle

172

(1)

Perspectives

173

(8)

Acknowledgments

174

(1)

Abbreviations and Definitions

174

(1)

References

175

(6)

Are There Proteins Containing Chromium?

181

(12)

R. Bruce Martin

Introduction

181

(4)

Enzymes/Proteins with Known Structure

185

(1)

Enzymes/Proteins with Unknown Structure

186

(1)

Perspectives

187

(6)

Abbreviations

188

(1)

References

188

(5)

Manganese-Containing Enzymes and Proteins

193

(76)

David C. Weatherburn

Introduction

196

(5)

Coordination Chemistry of Manganese

196

(1)

Manganese as an Oxidizing/Reducing Agent

197

(1)

Bioinorganic Role of Manganese

198

(1)

Homeostasis and Metabolism

198

(3)

Enzymes/Proteins with Known Structure

201

(29)

Oxidoreductases

201

(6)

Transferases

207

(5)

Hydrolases

212

(5)

Lyases

217

(2)

Isomerases

219

(5)

Ligases

224

(3)

Proteins Containing Bound Manganese

227

(3)

Manganese Enzymes with Unknown Structure

230

(10)

Oxidoreductases

231

(5)

Transferases

236

(1)

Hydrolases

237

(2)

Lyases

239

(1)

Isomerases

239

(1)

Ligases

240

(1)

Proteins Containing Bound Manganese

240

(1)

Structure-Function Relationships

240

(3)

Description of the Coordination Sphere of Manganese in Proteins

241

(1)

Description of Reaction Mechanisms

241

(2)

Perspectives and Outlook

243

(26)

Acknowledgments

244

(1)

Abbreviations

244

(2)

References

246

(23)

Iron in Heme and Related Proteins

269

(88)

Paola Turano

Yi Lu

Introduction

271

(15)

Coordination Chemistry of Heme

271

(8)

Biosynthesis of Heme

279

(6)

Bioinorganic Role of Heme

285

(1)

Enzymes and Proteins with Known Structure

286

(36)

Cytochromes

286

(11)

Globins

297

(3)

Nitrophorin

300

(1)

Heme-Based Biosensors

301

(2)

Catalases

303

(1)

Peroxidases

304

(9)

Cytochrome P450

313

(2)

Nitric Oxide Synthase

315

(1)

Hydroxylamine Oxidoreductase

316

(1)

Nitrite Reductase

317

(3)

Bacterioferritins

320

(1)

Heme Oxygenase

320

(2)

Enzymes/Proteins with Unknown Structure

322

(2)

Guanylyl Cyclase

322

(1)

Cystathionine β-Synthase

323

(1)

Indoleamine 2,3-Dioxygenase and Tryptophan 2,3-Dioxygenase

323

(1)

Structure-Function Relationships

324

(14)

Expression Systems

324

(2)

Detailed Structure-Function Relationships

326

(12)

Perspectives and Outlook

338

(19)

Why Heme? Evolutionary Aspects

338

(1)

An Outlook

339

(1)

Acknowledgments

340

(1)

Abbreviations

341

(1)

References

342

(15)

Iron-Sulfur Proteins

357

(2)

Detlef Bentrop

Francesco Capozzi

Claudio Luchinat

Introduction

359

(13)

Coordination Chemistry of Iron in Iron-Sulfur Proteins

359

(3)

Overview of Consensus Sequences and Structural Classification

362

(3)

Bioinorganic Roles of Clusters

365

(7)

Iron-Sulfur Proteins with Known Structures

372

(38)

Rubredoxins and Other Proteins with Mononuclear Iron-Sulfur Clusters

372

(3)

Rieske Proteins

375

(4)

2Fe-2S Ferredoxins

379

(2)

Ferredoxins with Fe3S4 and/or Fe4S4 Clusters

381

(6)

High Potential Iron-Sulfur Proteins

387

(2)

Aconitase and Iron Regulatory Proteins

389

(2)

Siroheme-Containing Proteins

391

(2)

Nitrogenase Iron Protein

393

(3)

Fe4S4 Cluster-Containing DNA Repair Enzymes

396

(3)

Glutamine Phosphoribosylpyrophosphate Amidotransferase

399

(2)

Trimethylamine Dehydrogenase

401

(1)

The ``Hybrid'' or ``Meatball'' Cluster

402

(4)

Fumarate Reductase and Succinate Dehydrogenase

406

(2)

Pyruvate: Ferredoxin Oxidoreductase

408

(2)

Relevant Iron-Sulfur Proteins with Unknown Structures

410

(6)

Ribonucleotide Reductase and Pyruvate Formate-Lyase Activase

410

(2)

Biotin Synthase and Related Systems

412

(1)

Ferredoxin: Thioredoxin Reductase

413

(1)

The Regulator of Fumarate and Nitrate Reduction (FNR)

414

(1)

The SoxR Protein

415

(1)

Structure-Function Relationships

416

(13)

The Role of the Cluster and the Protein Moieties in Electron Transfer by Iron-Sulfur Proteins

416

(5)

Fe3S4/Fe4S4 Interconversion

421

(3)

Fe4S4/Fe2S4 Conversions

424

(1)

Fe-Only Hydrogenases: The H Cluster

425

(3)

The Role of the Cluster in Folding and Stability of Iron-Sulfur Proteins

428

(1)

Perspectives

429

(1)

Evolutionary Aspects

429

(13)

Open Questions

442

(3)

Acknowledgments

445

(1)

Abbreviations and Definitions

446

(1)

References

447

(14)

Structure-Function of Nonheme Iron Proteins with Oxygen- and Nitrogen-Dominated Coordination

461

(571)

Par Nordlund

Introduction

463

(5)

Iron Homeostasis and Metabolism

463

(2)

Iron and Nonheme Iron Proteins

465

(3)

Iron-Oxygen/Nitrogen Protein Families

468

(3)

Structural and Mechanistic Studies of Iron-Oxygen/Nitrogen Proteins

470

(1)

Structure and Mechanisms of Iron-Oxygen/Nitrogen Proteins

471

(79)

Lipoxygenases

471

(7)

Intradiol Dioxygenases

478

(6)

Pterin-Dependent Hydroxylases

484

(7)

2-Oxoglutarate-Dependent Oxidases and Related Enzymes

491

(11)

Extradiol Dioxygenases and Related Enzymes

502

(9)

Dioxygenases Containing Rieske Centers

511

(5)

Hemerythrin

516

(3)

Large Diiron Carboxylate Proteins

519

(22)

Rubrerythrin

541

(3)

Nitrile Hydratases

544

(3)

Purple Acid Phosphatases

547

(3)

An Emerging View of the Structure-Function Relationship of Iron-Oxygen/Nitrogen Proteins

550

(21)

Effects of the Coordination Environment

552

(2)

Effects of Net Charge and Charge Distributions

554

(1)

Conformational Flexibility and the Control of O2 Reactivity

555

(1)

Geometries of the Activated O2 Species

556

(1)

Acknowledgments

557

(1)

Abbreviations and Definitions

558

(1)

References

559

(12)

Iron Storage and Transport Proteins

571

(32)

Fabio Arnesano

Alessandro Provenzani

Introduction

572

(1)

Proteins with Known Structure

573

(11)

Ferritins: Occurrence and Biological Role

573

(1)

Ferritins: Structural Classification

573

(2)

Structures of Ferritins

575

(3)

Transferrins: Occurrence and Biological Role

578

(1)

Transferrins: Structural Classification

578

(1)

Structures of Transferrins

579

(5)

Proteins with Unknown Structure

584

(1)

The Iron Pathway

584

(1)

Structure-Function Relationships

585

(8)

Expression Systems

585

(1)

Ferritins: Structure-Function Relationships

586

(4)

Transferrins: Structure-Function Relationships

590

(3)

Perspectives

593

(10)

Acknowledgments

593

(1)

Abbreviations and Definitions

594

(1)

References

594

(9)

Cobalt in Vitamin B12 and Its Enzymes

603

(66)

John M. Pratt

Introduction

605

(13)

Outline of Dates, Structures, and Reactions

605

(5)

Aims, Scope, and Organization of the Review

610

(1)

Nomenclature of Corrinoids

610

(1)

Basic Coordination Chemistry: Oxidation States, cis and trans Effects

611

(2)

Why Cobalt?

613

(2)

Why Corrin?

615

(3)

Enzymes with Known Structure: B12-Dependent Mutases

618

(13)

Reactions Catalyzed by Mutases (Isomerases)

619

(3)

Available Structures of Mutases

622

(1)

Major Structural Features: Domains, Modular Construction, and Evolution

623

(4)

Structural Features Relevant to the Mutase Reaction Mechanism

627

(3)

Summary of Main Points

630

(1)

B12-Binding Enzymes/Proteins with Unknown Structures

631

(6)

Distribution and Biosynthesis

631

(1)

Absorption, Transport, and Transformation of Cobalt Corrinoids

632

(2)

B12-Dependent Methyltransferases

634

(2)

Other Known or Possible B12-Dependent Enzymatic Reactions

636

(1)

Models, Mechanisms, and Structure-Function Relationships of the Mutases

637

(16)

Fission of the Co-C Bond: Mechanism for Applying Steric Distortion

638

(8)

The Co-Radical Charge-Transfer Complex

646

(1)

Rearrangement of the Substrate-Derived Radical

647

(5)

Summary of Main Points

652

(1)

Perspectives

653

(16)

B12-Dependent Mutases: Precis of Present Results

654

(3)

B12 in the Remote Past: Insights into Evolution

657

(2)

B12 in the Near Future: Problems and Prospects

659

(1)

Acknowledgments

660

(1)

Abbreviations

660

(2)

References

662

(7)

Nickel-Containing Enzymes

669

(40)

Stefano Ciurli

Stefano Mangani

Introduction

670

(1)

Bioinorganic Role of Nickel

670

(1)

Enzymes/Proteins with Known Structure

671

(12)

Urease

671

(4)

Hydrogenase

675

(5)

Methyl-Coenzyme M Reductase

680

(3)

Enzymes/Proteins with Unknown Structure

683

(6)

Carbon Monoxide Dehydrogenase/Acetyl-Coenzyme A Synthase

683

(2)

Nickel Superoxide Dismutase

685

(2)

Nickel Chaperonins

687

(2)

Structure-Function Relationships

689

(10)

Urease

689

(1)

[NiFe]-Hydrogenase

690

(3)

Methyl-Coenzyme M Reductase

693

(4)

Carbon Monoxide Dehydrogenase/Acetyl-Coenzyme A Synthase

697

(2)

Superoxide Dismutase

699

(1)

Future Perspectives

699

(10)

Abbreviations

700

(1)

References

700

(9)

Copper Proteins in the Transport and Activation of Dioxygen, and the Reduction of Inorganic Molecules

709

(54)

Malcolm A. Halcrow

Peter F. Knowles

Simon E. V. Phillips

Introduction

710

(5)

Coordination Chemistry of Copper

710

(1)

Bioinorganic Role of Copper

711

(2)

Homeostasis and Metabolism

713

(2)

Enzymes/Proteins with Known Structure

715

(15)

Galactose Oxidase

720

(1)

Amine Oxidases

721

(2)

Peptidylglycine α-Hydroxylating Monooxygenase

723

(2)

Hemocyanin

725

(1)

Catechol Oxidase

726

(1)

Cytochrome c Oxidase

727

(3)

Structural Features of Copper Oxidative Enzymes of Unknown 3D Structure

730

(4)

Lysyl Oxidase

730

(1)

Dopamine β-Monooxygenase

730

(1)

Tyrosinase

731

(1)

Methane Monooxygenase and Ammonia Monooxygenase

732

(1)

Nitrous Oxide Reductase

733

(1)

Structure-Function Relationships

734

(15)

Catalytic Mechanisms

734

(12)

Structure-Function Comparisons Between Enzymes

746

(3)

Perspectives and Outlook

749

(14)

Abbreviations and Definitions

751

(1)

References

751

(12)

Multi-Copper Oxidases

763

(50)

Peter F. Lindley

Introduction

764

(7)

Spectroscopic Classification of Copper Ions

765

(2)

The Cupredoxin Fold

767

(1)

The Overall Architecture of the Multi-Copper Oxidase Family

767

(4)

Known Structures in the Multi-Copper Oxidase Family

771

(8)

Ascorbate Oxidase

771

(1)

Laccase

772

(2)

Nitrite Reductase

774

(2)

Human Ceruloplasmin

776

(3)

Unknown Structures: Coagulation Factors V and VIII

779

(1)

Roles of Factors V and VIII in Blood Coagulation

779

(1)

Overall Configuration of Factor V and VIII Molecules

779

(1)

A Model for Factor VIII Based on Human Ceruloplasmin

780

(1)

Structure-Function Relationships

780

(21)

The Copper Binding Sites

780

(7)

Organic Substrate Binding Sites in Ascorbate Oxidase and Laccase

787

(1)

Mechanism of Oxygen Reduction by the Trinuclear Copper Center

788

(3)

Azide Inhibition in Ascorbate Oxidase and Human Ceruloplasmin

791

(3)

Ceruloplasmin and Ferroxidase Activity

794

(3)

Binding of Organic Substrates to Human Ceruloplasmin

797

(3)

Ceruloplasmin and Hemosiderosis

800

(1)

Perspectives

801

(12)

Evolutionary Aspects of the Multi-Copper Oxidase Family

801

(4)

Open Questions

805

(1)

Acknowledgments

806

(1)

Abbreviations and Definitions

806

(1)

References

807

(6)

Copper in Electron-Transfer Proteins

813

(44)

Alejandro J. Vila

Claudio O. Fernandez

Introduction

814

(2)

Proteins with Known Structure

816

(17)

The Cupredoxin Fold

816

(2)

Blue Copper Proteins

818

(12)

Blue Oxidases

830

(1)

Nitrite Reductase

831

(1)

The Binuclear CuA Site

832

(1)

Proteins with Unknown Structure

833

(2)

Blue Copper Proteins

833

(1)

Blue Oxidases

834

(1)

N2O Reductase

835

(1)

Structure-Function Relationships

835

(6)

Description of the Coordination Sphere of the Metal Ions

835

(1)

Spectroscopic Studies

836

(2)

Mutagenesis Studies

838

(1)

Redox Potentials

839

(1)

Electron Transfer Mechanisms

840

(1)

Perspectives

841

(16)

Acknowledgments

842

(1)

Abbreviations and Definitions

842

(1)

References

843

(14)

Proteins of Various Functions Containing Copper

857

(24)

Peter F. Lindley

Introduction

858

(1)

Known X-Ray Structures: Albumin and Copper, Zinc Superoxide Dismutase

858

(2)

Serum Albumin

858

(2)

Cu,Zn Superoxide Dismutase

860

(1)

Known NMR Structures: Metallothioneins and Menkes' Copper-Transporting ATPases

860

(2)

Metallothioneins

860

(2)

Menkes' Cu-Transporting ATPases

862

(1)

Structure-Function Relationships

862

(12)

Copper Binding Sites in Serum Albumin

862

(1)

Structure-Function Relationships in Superoxide Dismutase

863

(9)

Copper Binding Sites in Metallothioneins

872

(1)

Copper Binding Site in the Menkes' Cu-Transporting ATPase

873

(1)

Perspectives: The Copper Chaperones

874

(7)

Acknowledgments

874

(1)

Abbreviations and Definitions

875

(2)

References

877

(4)

Zinc Sites in Metalloenzymes and Related Proteins

881

(80)

David S. Auld

Introduction

882

(2)

A Growing Awareness of Zinc in Biology

882

(1)

Zinc Chemistry: Ideal for its Varied Functions

883

(1)

Classification of Zinc Sites in Metalloenzymes and Related Proteins

884

(23)

Catalytic Zinc Sites

885

(6)

Structural Zinc Sites

891

(2)

Cocatalytic Zinc Sites

893

(9)

Protein Interface Zinc Sites

902

(5)

Tracking Zinc Enzymes through Their Putative Zinc Binding Sites

907

(10)

Determination of the Number of Zinc Enzymes

907

(2)

Zinc Binding Site Motifs as a Means for the Discovery of New Zinc Families

909

(6)

Mutagenesis as a Means of Detecting New Zinc Binding Sites

915

(2)

Structure-Function Relationships

917

(24)

Inactivation of Metalloenzyme Catalysis

917

(7)

Effect of Scaffolding on Catalytic Activity

924

(7)

Mechanistic Studies of Catalytic Zinc Sites

931

(6)

Mechanistic Studies of Cocatalytic Zinc Sites

937

(4)

Concluding Remarks

941

(20)

Abbreviations and Definitions

942

(1)

References

943

(18)

Zinc Finger Proteins

961

(40)

Gert E. Folkers

Hiroyoki Hanzawa

Rolf Boelens

Introduction

962

(2)

Historical Perspectives

962

(1)

Definition of Zinc Finger Domains

962

(1)

Focus of this Chapter

963

(1)

Zinc Finger Proteins with Known Structure

964

(18)

Zinc Finger Domains Containing One Zinc

964

(12)

Double-Zinc-Finger Proteins

976

(5)

Membrane-Binding Double-Zinc-Finger Domains

981

(1)

Zinc Fingers with Unknown Structure

982

(3)

Structure-Function Relationships

985

(4)

Evolutionary Aspects

985

(4)

Perspectives

989

(12)

Abbreviations

990

(2)

References

992

(9)

Other Zinc Proteins: Metallothioneins and Insulin

1001

(22)

Elena Babini

Maria Silvia Viezzoli

Introduction

1002

(1)

Proteins with Known Structure

1002

(10)

Metallothioneins: Occurrence and Biological Role

1002

(1)

Metallothioneins: Structural Classification

1003

(1)

Structure of Human, Rabbit, Rat, and Mouse Metallothioneins

1003

(3)

Structure of Blue Crab Metallothionein

1006

(1)

Structure of Purple Sea Urchin Metallothionein

1007

(1)

Insulin: Occurrence and Biological Role

1007

(1)

Insulin: Structural Classification

1008

(1)

Insulin: Structure

1009

(3)

Proteins with Unknown Structure

1012

(2)

The Human Neuronal Growth Inhibitory Factor (Metallothionein-3)

1012

(1)

Phytochelatins

1013

(1)

Cod Insulin

1013

(1)

Expression Systems

1013

(1)

Structure-Function Relationships

1014

(2)

Metallothioneins

1014

(1)

Insulin: Relationship between Conformational Transitions and Biological Function

1015

(1)

Perspectives

1016

(7)

Metallothioneins

1016

(1)

Insulin

1016

(1)

Abbreviations and Definitions

1016

(1)

References

1017

(6)

Enzymes and Proteins Containing Molybdenum or Tungsten

1023

(68)

C. David Garner

Russell Banham

Serena J. Cooper

E. Stephen Davies

Lisa J. Stewart

Introduction

1024

(10)

Perspective

1024

(1)

Cofactors

1025

(4)

Molybdenum vs. Tungsten

1029

(1)

Coordination Chemistry of Molybdenum and Tungsten Relevant to Their Biological Functions

1030

(4)

Proteins and Enzymes with Known Structure

1034

(29)

Molybdate and Tungstate Transport Proteins

1034

(1)

Nitrogenases

1035

(3)

Molybdenum Oxotransferases

1038

(21)

Tungstoenzymes

1059

(4)

Enzymes with Unknown Structure

1063

(6)

Structure-Function Relationships

1069

(3)

Expression Systems

1069

(1)

Coordination Sphere of the Metal Ions

1070

(1)

Reaction Mechanisms

1071

(1)

Perspectives

1072

(19)

Acknowledgments

1072

(1)

Abbreviations

1072

(2)

References

1074

(17)

Emerging Themes and Patterns Among Metalloproteins

1091

(28)

John M. Pratt

Introduction

1092

(6)

A Half Century of Bioinorganic Chemistry

1092

(2)

Some Emerging Themes

1094

(4)

Focus on the Protein: Conformation Changes

1098

(5)

MgATPase: The World's Smallest Rotary Engine

1098

(1)

B12-Dependent Mutases: A Molecular Nutcracker

1099

(1)

Lessons for Enzymic Catalysis

1100

(3)

Focus on the Metal: Metal Specificity

1103

(8)

Co(III) + CH3-: Metal-Ligand Covalency and the Use of 4s Orbitals

1104

(1)

Fe(II) + NH3: Donor Ligands and Coulombic/Solvation Effects

1104

(2)

Fe(II) + O2: Acceptor Ligands

1106

(1)

Fe(II) + CO:??

1107

(1)

Usage = Reactivity x Availability: Cr, Co, Cu

1108

(3)

Conclusions

1111

(8)

Abbreviations

1113

(1)

References

1114

(5)

Subject Index

1119

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Handbook on Metalloproteins

Summary

Table of Contents

Supplemental Materials