Preface to the Series |
Preface to Volume 39 |
In Memoriam of Professor Robert C. Bray |
Contributors |
Contents of Previous Volumes |
Handbook on Toxicity of Inorganic Compounds |
Handbook on Metals in Clinical and Analytical Chemistry |
Handbook on Metalloproteins |
The Biogeochemistry of Molybdenum and Tungsten / Edward I. StiefelChapter 1: |
Introduction / 1.: |
Molybdenum and Tungsten in the Environment / 2.: |
The Nitrogen Cycle / 3.: |
Sulfur Metabolism and the Sulfur Cycle / 4.: |
Carbon Metabolism / 5.: |
Arsenic, Selenium, and Chlorine Metabolism / 6.: |
Conclusion / 7.: |
Acknowledgment |
Abbreviations |
References |
Transport, Homeostasis, Regulation, and Binding of Molybdate and Tungstate to Proteins / Richard N. Pau ; David M. LawsonChapter 2: |
Competition with Iron(III) |
Transport Systems |
Cytoplasmic Molybdate-Binding Proteins |
Conclusions |
Acknowledgments |
Abbreviations and Definitions |
Molybdenum Nitrogenases: A Crystallographic and Mechanistic View / Barry E. SmithChapter 3: |
The Nitrogenases |
The Molybdenum-Iron Protein |
The Iron Protein |
Mechanistic Studies |
The Nitrogenase Complex |
The Active Site |
Chemical Dinitrogen Fixation by Molybdenum and Tungsten Complexes: Insights From Coordination Chemistry / Masanobu Hidai ; Yasushi Mizobe8.: |
Preparation and Structures of Dinitrogen Complexes |
Reactions of Coordinated Dinitrogen |
Biosynthesis of the Nitrogenase Iron-Molybdenum-Cofactor From Azotobacter Vinelandii / Jeverson Frazzon ; Dennis R. DeanChapter 5: |
Biochemical Genetic Analysis of FeMo Cofactor Biosynthesis |
A General Model for FeMo Cofactor Biosynthesis |
Mobilization of Iron and Sulfur |
NifB Cofactor |
The NifEN Complex |
Homocitrate Formation and Molybdenum Insertion |
Role of Intermediate Carriers in FeMo Cofactor Biosynthesis |
Role of the Iron Protein in Cofactor Assembly / 9.: |
Summary and Future Prospects / 10.: |
Molybdenum Enzymes Containing the Pyranopterin Cofactor: an Overview / Russ HilleChapter 6: |
Classification of the Mononuclear Molybdenum Enzymes |
Consideration of Selected Enzymes Not Covered in Other Chapters |
Mechanistic Considerations |
Concluding Remarks |
The Molybdenum and Tungsten Cofactors: A Crystallographic View / Holger Dobbek ; Robert HuberChapter 7: |
Structure of the Mo/W Cofactor |
Moco-Containing Enzyme Families |
Limitations of a Crystallographic Model |
Models for the Pyranopterin-Containing Molybdenum and Tungsten Cofactors / Berthold Fischer ; Sharon J. Nieter BurgmayerChapter 8: |
Early Models |
Model Complexes of 1,2-Ene-Dithiolates |
Metal Complexes of Pterins |
Models with All Three Redox Sites |
Biosynthesis and Molecular Biology of the Molybdenum Cofactor (Moco) / Ralf R. Mendel ; Gunter SchwarzChapter 9: |
Genetics of the Molybdenum Cofactor |
Biosynthesis of the Molybdenum Cofactor |
Regulation of Molybdenum Cofactor Synthesis |
Molybdenum in Nitrate Reductase and Nitrite Oxidoreductase / Peter M. H. Kroneck ; Dietmar J. AbtChapter 10: |
Bacterial Respiratory Chains, Metalloenzymes, and Bioenergetics |
Nitrate Reductase |
Nitrite Oxidoreductase |
Environmental Aspects and Biosensors |
The Molybdenum-Containing Hydroxylases of Nicotinate, Isonicotinate, and Nicotine / Jan R. Andreesen ; Susanne FetznerChapter 11: |
Hydroxylations of Nicotinate and Derivatives |
Catabolism of Isonicotinate and Derivatives |
Nicotine Catabolism: Enzymes and Genes Involved in Aerobic Transformations |
Biotechnological Potentials and Medical Implications |
The Molybdenum-Containing Xanthine Oxidoreductases and Picolinate Dehydrogenases / Emil F. Pai ; Takeshi NishinoChapter 12: |
Xanthine Dehydrogenase/Xanthine Oxidase |
Picolinate Dehydrogenase |
Enzymes of the Xanthine Oxidase Family: the Role of Molybdenum / David J. LoweChapter 13: |
The Reactions Catalyzed |
Spectroscopic Investigations |
Kinetic Studies |
Theoretical Calculations |
Discussion |
The Molybdenum-Containing Hydroxylases of Quinoline, Isoquinoline, and Quinaldine / Reinhard Kappl ; Jurgen HuttermannChapter 14: |
Biochemical and Genetic Characterization |
Structural Features of Related Enzymes |
EPR and ENDOR Characterization of Redox Centers |
Molybdenum Enzymes in Reactions Involving Aldehydes and Acids / Maria Joao Romao ; Carlos A. Cunha ; Carlos D. Brondino ; Jose J. G. MouraChapter 15: |
Enzymes of the Xanthine Oxidase Family |
Enzymes of the Aldehyde Oxidoreductase Family |
Molybdenum and Tungsten Enzymes in C1 Metabolism / Julia A. Vorholt ; Rudolf K. ThauerChapter 16: |
Formate Dehydrogenase |
Formylmethanofuran Dehydrogenase |
Carbon Monoxide Dehydrogenase |
Formaldehyde Dehydrogenases |
Molybdenum Enzymes and Sulfur Metabolism / John H. Enemark ; Michele Mader CosperChapter 17: |
Sulfite Oxidase |
Dimethyl Sulfoxide Reductase |
Biotin Sulfoxide Reductase |
Polysulfide Reductase |
Comparison of Selenium-Containing Molybdoenzymes / Vadim N. GladyshevChapter 18: |
Overview of Selenium-Containing Molybdoenzymes |
Incorporation of Selenium into Molybdoenzymes |
Selenium Versus Sulfur in Catalysis |
Evolution of Selenocysteine-Containing Molybdoenzymes |
Tungsten-Dependent Aldehyde Oxidoreductase: A New Family of Enzymes Containing the Pterin Cofactor / Roopali Roy ; Michael W. W. AdamsChapter 19: |
Classification of Tungstoenzymes |
Aldehyde Ferredoxin Oxidoreductase |
Carboxylic Acid Reductase and Aldehyde Dehydrogenase |
Formaldehyde Ferredoxin Oxidoreductase |
Glyceraldehyde-3-Phosphate Ferredoxin Oxidoreductase |
Hypothetical Tungstoenzymes--WOR4 and WOR5 |
Tungsten Versus Molybdenum in the AOR Family |
Tungsten-Substituted Molybdenum Enzymes / C. David Garner ; Lisa J. StewartChapter 20: |
Molybdenum and Tungsten Chemistry: Similarities and Differences |
Molybdenum and Tungsten Geochemistry and Link to Bioavailability |
Early Attempts to Substitute Tungsten for Molybdenum |
Molybdenum-Substituted Tungsten Acetylene Hydratase |
Molybdenum Metabolism and Requirements in Humans / Judith R. TurnlundChapter 21: |
Essentiality of Molybdenum in Humans |
Dietary Intake and Bioavailability of Molybdenum |
Molybdenum Deficiency and Toxicity |
Stable Isotope Studies of Molybdenum Metabolism |
Metabolism and Toxicity of Tungsten in Humans and Animals / Florence Lagarde ; Maurice LeroyChapter 22: |
Metabolism of Tungsten |
Toxicity of Tungsten |
Subject Index |
Preface to the Series |
Preface to Volume 39 |
In Memoriam of Professor Robert C. Bray |