Metals Ions in Biological System: Volume 39: Molybdenum and Tungsten: Their Roles in Biological Processes:

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ISBN: 9780824707651 | 0824707656
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Copyright: 3/6/2002

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Volume 39: Molybdenum and Tungsten: Their Roles in Biological Processes is devoted soley to the vital research area on molybdenum and tungsten and their role in biology. It offers a comprehensive and timely account of this fascinating topic by 40 distinguished international authorities. Topics include: transport, homeostasis, regulation and binding of molybdate and tungstate to proteins, crystallographic characterization, coordination of complexes, and biosynthesis.

Preface to the Series

iii

Preface to Volume 39

In Memoriam of Professor Robert C. Bray

vii

Contributors

xxiii

Contents of Previous Volumes

xxvii

Handbook on Toxicity of Inorganic Compounds

lix

Handbook on Metals in Clinical and Analytical Chemistry

lix

Handbook on Metalloproteins

lix

The Biogeochemistry Of Molybdenum And Tungsten

(30)

Edward I. Stiefel

Introduction

(1)

Molybdenum and Tungsten in the Environment

(4)

The Nitrogen Cycle

(4)

Sulfur Metabolism and the Sulfur Cycle

(6)

Carbon Metabolism

(2)

Arsenic, Selenium, and Chlorine Metabolism

(2)

Conclusion

(10)

Acknowledgment

(1)

Abbreviations

(1)

References

(8)

Transport, Homeostasis, Regulation, and Binding of Molybdate and Tungstate to Proteins

(44)

Richard N. Pau

David M. Lawson

Introduction

(2)

Competition with Iron(III)

(5)

Transport Systems

(10)

Cytoplasmic Molybdate-Binding Proteins

(16)

Conclusions

(10)

Acknowledgments

(1)

Abbreviations and Definitions

(1)

References

(7)

Molybdenum Nitrogenases: A Crystallographic and Mechanistic View

(46)

David M. Lawson

Barry E. Smith

Introduction

(1)

The Nitrogenases

(4)

The Molybdenum-Iron Protein

(6)

The Iron Protein

(3)

Mechanistic Studies

(4)

The Nitrogenase Complex

(4)

The Active Site

(11)

Conclusions

109

(12)

Acknowledgments

110

(1)

Abbreviations and Definitions

110

(1)

References

111

(10)

Chemical Dinitrogen Fixation by Molybdenum and Tungsten Complexes: Insights From Coordination Chemistry

121

(42)

Masanobu Hidai

Yasushi Mizobe

Introduction

122

(2)

Preparation and Structures of Dinitrogen Complexes

124

(6)

Reactions of Coordinated Dinitrogen

130

(24)

Conclusions

154

(9)

Abbreviations

155

(1)

References

155

(8)

Biosynthesis of the Nitrogenase Iron-Molybdenum-Cofactor from Azotobacter Vinelandii

163

(24)

Jeverson Frazzon

Dennis R. Dean

Introduction

164

(3)

Biochemical Genetic Analysis of FeMo Cofactor Biosynthesis

167

(2)

A General Model for FeMo Cofactor Biosynthesis

169

(1)

Mobilization of Iron and Sulfur

170

(1)

NifB Cofactor

171

(4)

The NifEN Complex

175

(1)

Homocitrate Formation and Molybdenum Insertion

176

(3)

Role of Intermediate Carriers in FeMo Cofactor Biosynthesis

179

(2)

Role of the Iron Protein in Cofactor Assembly

181

(1)

Summary and Future Prospects

182

(5)

Acknowledgments

183

(1)

Abbreviations

183

(1)

References

183

(4)

Molybdenum Enzymes Containing the Pyranopterin Cofactor: An Overview

187

(40)

Russ Hille

Introduction

188

(7)

Classification of the Mononuclear Molybdenum Enzymes

195

(10)

Consideration of Selected Enzymes Not Covered in Other Chapters

205

(6)

Mechanistic Considerations

211

(7)

Concluding Remarks

218

(9)

Acknowledgment

219

(1)

Abbreviations

219

(1)

References

219

(8)

The Molybdenum and Tungsten Cofactors: A Crystallographic View

227

(38)

Holger Dobbek

Robert Huber

Introduction

228

(1)

Structure of the Mo/W Cofactor

229

(3)

Moco-Containing Enzyme Families

232

(24)

Limitations of a Crystallographic Model

256

(9)

Acknowledgments

258

(1)

Abbreviations and Definitions

259

(1)

References

260

(5)

Models for the Pyranopterin-Containing Molybdenum and Tungsten Cofactors

265

(52)

Berthold Fischer

Sharon J. Nieter Burgmayer

Introduction

266

(6)

Early Models

272

(6)

Model Complexes of 1,2-Ene-Dithiolates

278

(9)

Metal Complexes of Pterins

287

(8)

Models with All Three Redox Sites

295

(8)

Conclusion

303

(14)

Acknowledgments

304

(1)

Abbreviations

304

(1)

References

305

(12)

Biosynthesis and Molecular, Biology of the Molybdenum Cofactor (Moco)

317

(52)

Ralf R. Mendel

Gunter Schwarz

Introduction

318

(4)

Genetics of the Molybdenum Cofactor

322

(2)

Biosynthesis of the Molybdenum Cofactor

324

(32)

Regulation of Molybdenum Cofactor Synthesis

356

(2)

Conclusions

358

(11)

Acknowledgments

359

(1)

Abbreviations

359

(1)

References

359

(10)

Molybdenum in Nitrate Reductase and Nitrite Oxidoreductase

369

(36)

Peter M. H. Kroneck

Dietmar J. Abt

Introduction

370

(3)

Bacterial Respiratory Chains, Metalloenzymes, and Bioenergetics

373

(6)

Nitrate Reductase

379

(12)

Nitrite Oxidoreductase

391

(3)

Environmental Aspects and Biosensors

394

(11)

Acknowledgments

395

(1)

Abbreviations and Definitions

395

(1)

References

396

(9)

The Molybdenum-Containing Hydroxylases of Nicotinate, Isonicotinate, and Nicotine

405

(26)

Jan R. Andreesen

Susanne Fetzner

Introduction

406

(1)

Hydroxylations of Nicotinate and Derivatives

407

(8)

Catabolism of Isonicotinate and Derivatives

415

(3)

Nicotine Catabolism: Enzymes and Genes Involved in Aerobic Transformations

418

(3)

Biotechnological Potentials and Medical Implications

421

(2)

Conclusions

423

(8)

Acknowledgments

423

(1)

Abbreviations

423

(1)

References

424

(7)

The Molybdenum-Containing Xanthine Oxidoreductases and Picolinate Dehydrogenases

431

(24)

Emil F. Pai

Takeshi Nishino

Introduction

432

(3)

Xanthine Dehydrogenase/Xanthine Oxidase

435

(12)

Picolinate Dehydrogenase

447

(1)

Conclusions

448

(7)

Acknowledgments

449

(1)

Abbreviations

449

(1)

References

449

(6)

Enzymes of the Xanthine Oxidase Family: The Role of Molybdenum

455

(26)

David J. Lowe

Introduction

456

(2)

The Reactions Catalyzed

458

(4)

Spectroscopic Investigations

462

(7)

Kinetic Studies

469

(1)

Theoretical Calculations

470

(2)

Discussion

472

(3)

Conclusions

475

(6)

Acknowledgment

475

(1)

Abbreviations

475

(1)

References

476

(5)

The Molybdenum-Containing Hydroxylases of Quinoline, Isoquinoline, and Quinaldine

481

(58)

Reinhard Kappl

Jurgen Huttermann

Susanne Fetzner

Introduction

482

(1)

Biochemical and Genetic Characterization

483

(11)

Structural Features of Related Enzymes

494

(3)

EPR and ENDOR Characterization of Redox Centers

497

(33)

Conclusions

530

(9)

Acknowledgments

530

(1)

Abbreviations

530

(1)

References

531

(8)

Molybdenum Enzymes in Reactions Involving Aldehydes and Acids

539

(32)

Maria Joao Romao

Carlos A. Cunha

Carlos D. Brondino

Jose J. G. Moura

Introduction

540

(1)

Enzymes of the Xanthine Oxidase Family

541

(18)

Enzymes of the Aldehyde Oxidoreductase Family

559

(6)

Conclusions

565

(6)

Acknowledgments

566

(1)

Abbreviations

566

(1)

References

567

(4)

Molybdenum and Tungsten Enzymes in C1 Metabolism

571

(50)

Julia A. Vorholt

Rudolf K. Thauer

Introduction

572

(3)

Formate Dehydrogenase

575

(12)

Formylmethanofuran Dehydrogenase

587

(8)

Carbon Monoxide Dehydrogenase

595

(3)

Formaldehyde Dehydrogenases

598

(3)

Conclusions

601

(20)

Acknowledgments

602

(1)

Abbreviations and Definitions

602

(1)

References

603

(18)

Molybdenum Enzymes and Sulfur Metabolism

621

(34)

John H. Enemark

Michele Mader Cosper

Introduction

622

(1)

Sulfite Oxidase

623

(12)

Dimethyl Sulfoxide Reductase

635

(7)

Biotin Sulfoxide Reductase

642

(2)

Polysulfide Reductase

644

(1)

Conclusions

645

(10)

Acknowledgments

645

(1)

Abbreviations and Definitions

646

(1)

References

647

(8)

Comparison of Selenium-Containing Molybdoenzymes

655

(18)

Vadim N. Gladyshev

Introduction

656

(2)

Overview of Selenium-Containing Molybdoenzymes

658

(4)

Incorporation of Selenium into Molybdoenzymes

662

(2)

Selenium Versus Sulfur in Catalysis

664

(3)

Evolution of Selenocysteine-Containing Molybdoenzymes

667

(1)

Conclusions

668

(5)

Acknowledgments

669

(1)

Abbreviations

669

(1)

References

670

(3)

Tungsten-Dependent Aldehyde Oxidoreductase: A New Family of Enzymes Containing the Pterin Cofactor

673

(26)

Roopali Roy

Michael W. W. Adams

Introduction

674

(3)

Classification of Tungstoenzymes

677

(3)

Aldehyde Ferredoxin Oxidoreductase

680

(5)

Carboxylic Acid Reductase and Aldehyde Dehydrogenase

685

(2)

Formaldehyde Ferredoxin Oxidoreductase

687

(3)

Glyceraldehyde-3-Phosphate Ferredoxin Oxidoreductase

690

(1)

Hypothetical Tungstoenzymes-WOR4 and WOR5

691

(1)

Tungsten Versus Molybdenum in the AOR Family

692

(1)

Conclusions

693

(6)

Acknowledgment

694

(1)

Abbreviations

694

(1)

References

695

(4)

Tungsten-Substituted Molybdenum Enzymes

699

(28)

C. David Garner

Lisa J. Stewart

Introduction

700

(1)

Molybdenum and Tungsten Chemistry: Similarities and Differences

701

(3)

Molybdenum and Tungsten Geochemistry and Link to Bioavailability

704

(1)

Early Attempts to Substitute Tungsten for Molybdenum

705

(2)

Tungsten-Substituted Molybdenum Enzymes

707

(12)

Molybdenum-Substituted Tungsten Acetylene Hydratase

719

(1)

Conclusions

720

(7)

Abbreviations

721

(1)

References

722

(5)

Molybdenum Metabolism and Requirements in Humans

727

(14)

Judith R. Turnlund

Introduction

728

(1)

Essentiality of Molybdenum in Humans

728

(1)

Dietary Intake and Bioavailability of Molybdenum

729

(2)

Molybdenum Deficiency and Toxicity

731

(2)

Stable Isotope Studies of Molybdenum Metabolism

733

(3)

Conclusions

736

(5)

Abbreviations

736

(1)

References

736

(5)

Metabolism and Toxicity of Tungsten in Humans and Animals

741

(20)

Florence Lagarde

Maurice Leroy

Introduction

742

(1)

Metabolism of Tungsten

742

(10)

Toxicity of Tungsten

752

(3)

Conclusions

755

(6)

Abbreviations and Definitions

755

(1)

References

756

(5)

Subject Index

761

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Metals Ions in Biological System: Volume 39: Molybdenum and Tungsten: Their Roles in Biological Processes:

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