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1.

図書
図書
1. Methods involving metal ions and complexes in clinical chemistry
edited by Helmut Sigel ; with the assistance of Astrid Sigel
出版情報: New York : M. Dekker, c1983  xxv, 397 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 16
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2.

図書
図書
2. Vanadium and its role in life
edited by Helmut Sigel and Astrid Sigel
出版情報: New York : Marcel Dekker, c1995  xxxix, 779 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 31
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Inorganic considerations on the function of vanadium in biological systems
solution properties of vanadium(III) with regard to biological systems
the vanadyl ion - molecular structure of co-ordinating ligands by electron paramagnetic resonance and electron nuclear resonance-spectroscopy
vanadyl(IV) complexes of nucleotides
interactions of vanadates(V) with biogenic ligands
use of vanadate-induced photocleavage for detecting phosphate-binding sites in proteins
vanadium-protein by
Inorganic considerations on the function of vanadium in biological systems
solution properties of vanadium(III) with regard to biological systems
the vanadyl ion - molecular structure of co-ordinating ligands by electron paramagnetic resonance and electron nuclear resonance-spectroscopy
3.

図書
図書
3. Metalloenzymes involving amino acid-residue and related radicals
edited by Helmut Sigel and Astrid Sigel
出版情報: New York : Marcel Dekker, c1994  xxxiii, 494 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 30
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Preface to the Series
Preface to Volume 30
Contributors
Contents of Previous Volumes
Handbook on Toxicity of Inorganic Compounds
Handbook on Metals in Clinical and Analytical Chemistry
Free Radicals and Metalloenzymes: General Considerations / Ei-Ichiro OchiaiChapter 1：
Introduction: A Survey of Biologically Relevant Free Radicals / 1.：
Necessity of Free Radicals and Metal Ions / 2.：
Reactivities of Free Radicals / 3.：
Summary of Free Radical-Dependent Metalloenzymes / 4.：
Abbreviations
References
Peroxidases: Structure, Function, and Engineering / Thomas L. Poulos ; Roger E. FennaChapter 2：
Introduction
Peroxidase Crystal Structures
Peroxidase Catalytic Mechanisms
Peroxidase Engineering
Conclusions / 5.：
Photosystem II / Curtis W. Hoganson ; Gerald T. BabcockChapter 3：
Identification and Spectroscopic Studies of the Tyrosine Radicals
Electron Transfer Reactions of the Tyrosine Radicals--Both O[subscript 2]-Evolving and Inhibited Photosystem II
Other Radicals in Photosystem II
Concluding Remarks
Ribonucleotide Reductase in Mammalian Systems / Lars Thelander ; Astrid GraslundChapter 4：
Mammalian Ribonucleotide Reductase
Herpes Simplex Virus Ribonucleotide Reductase
Comparison of Amino Acid Sequences and Spectroscopic Properties for Different Species
Formation, Properties, and Stability of the Fe-Tyrosyl Radical Center
Inhibitors; Radical Scavengers; Iron Chelators; Specific Peptides / 6.：
Subunit Interaction and Electron Transfer / 7.：
Manganese-Dependent Ribonucleotide Reduction and Overproduction of Nucleotides in Coryneform Bacteria / Georg Auling ; Hartmut FollmannChapter 5：
Introduction: The Diversity of Ribonucleotide Reductase Systems
Effects of Manganese Depletion in Coryneform Bacteria
The Manganese-Containing Ribonucleotide Reductase of Brevibacterium ammoniagenes
Distribution of Manganese Ribonucleotide Reductases
Concluding Remarks--Ribonucleotide Reduction: Universal but Not Uniform
Prostaglandin Endoperoxide Synthases / William L. Smith ; Lawrence J. MarnettChapter 6：
PGH Synthase Isozymes
Cyclooxygenase Catalysis
Peroxidase Catalysis
Cyclooxygenase-Peroxidase Interrelationships
PGH Synthase Structure
Diol Dehydrase from Clostridium Glycolicum: The Non-B[subscript 12]-Dependent Enzyme / Maris G. N. HartmanisChapter 7：
Diol Metabolism in C. glycolicum
Properties of Membrane bound Diol Dehydrase from C. glycolicum
Characterization of Diol Dehydrase
Diol Dehydrase and Glycerol Dehydrase, Coenzyme B[subscript 12]-Dependent Isozymes / Tetsuo TorayaChapter 8：
Purification, Properties, and Structures
Catalytic Properties and Mechanism of Action
Formation of Free Radicals
Inactivation and Reactivation
Physiological Roles
Adenosylcobalamin (Vitamin B[subscript 12] Coenzyme)-Dependent Enzymes / Chapter 9：
Survey of Adenosylcobalamin-Dependent Enzymes
Mechanisms of the Co-C Bond Cleavage
Mechanisms of the Subsequent Reactions
Conclusion
S-Adenosylmethionine-Dependent Radical Formation in Anaerobic Systems / Kenny K. Wong ; John W. KozarichChapter 10：
Pyruvate Formate Lyase-Activating Enzyme
Lysine 2,3-Aminomutase
Anaerobic Ribonucleotide Reductase
The Free Radical-Coupled Copper Active Site of Galactose Oxidase / James W. WhittakerChapter 11：
Historical Survey
Recent Developments
Model Reactions and the Role of the Radical in Catalysis
Abbreviations and Definitions
Amine Oxidases / Peter F. Knowles ; David M. DooleyChapter 12：
Structural Properties of Amine Oxidases
Catalytic Mechanism of Amine Oxidases
Biological Roles of Amine Oxidases
Conclusions and Prospects
Bacterial Transport of and Resistance to Copper / Nigel L. Brown ; Barry T. O. Lee ; Simon SilverChapter 13：
Copper in Bacterial Nutrition
Copper Transport and Uptake
Bacterial Systems Conferring Resistance to Excess Copper
Definitions and Abbreviations
Author Index
Subject Index
Preface to the Series
Preface to Volume 30
Contributors
4.

図書
図書
4. Molybdenum and tungsten : their roles in biological processes
edited by Astrid Sigel and Helmut Sigel
出版情報: New York : Marcel Dekker, c2002  lix, 810 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 39
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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
5.

図書
図書
5. The lanthanides and their interrelations with biosystems
edited by Astrid Sigel and Helmut Sigel
出版情報: New York : Marcel Dekker, c2003  lvii, 799 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 40
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6.

図書
図書
6. Probing of proteins by metal ions and their low-molecular-weight complexes
edited by Astrid Sigel and Helmut Sigel
出版情報: New York : M. Dekker, c2001  xlviii, 690 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 38
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目次情報: 続きを見る
Preface to the Series
Preface to Volume 38
Contributors
Contents of Previous Volumes
Handbook on Toxicity of Inorganic Compounds
Handbook on Metals in Clinical and Analytical Chemistry
Handbook on Metalloproteins
Peptide Bond Characteristics / R. Bruce MartinChapter 1：
Background / 1.：
Proton Binding and Loss / 2.：
Metal Ion Binding at the Peptide Bond / 3.：
Free Energies of Peptide Bond Hydrolysis and Formation / 4.：
Equilibrium Constants for Peptide Bond Formation in the Presence of Metal Ions / 5.：
Peptide Oxygen Basicity Determined by Amide Amino Group Basicity / 6.：
Metal Ion Effects on Rates of Peptide Bond Hydrolysis / 7.：
References
Lanthanide Ion-Mediated Peptide Hydrolysis / Makoto KomiyamaChapter 2：
Introduction
Amide Hydrolysis by Lanthanide Ions
Mechanism of Ce(IV) Catalysis
Cyclodextrin Complexes of Lanthanide Ions for Homogeneous Hydrolysis of Amides
Relevance of the Lanthanide-Mediated Amide Hydrolysis to DNA Hydrolysis
Conclusion
Acknowledgment
Abbreviations
Co(III)-Promoted Hydrolysis of Amides and Small Peptides / David A. Buckingham ; Charles R. ClarkChapter 3：
Early Studies and Scope
Co(III) Linkage Isomers and Isomerization
Hydrolysis by Direct Polarization
Bimolecular Reactions of Co-OH[subscript 2]/OH
Intramolecular Reactions of CoOH[subscript 2]/OH
Kinetic Parameters and Reaction Mechanism
Related Nonmetal Hydrolysis Reactions / 8.：
Synthetic Cu(II) and Ni(II) Peptidases / Gregory M. Polzin ; Judith N. BurstynChapter 4：
Hydrolysis of Simple Peptides by Cu(II) and Ni(II) Ions in Solution
Cleavage of Substrates Containing a Metal Binding Site by Cu(II) and Ni(II) Ions
Cleavage of Amides, Peptides, and Proteins by Defined Metal Complexes
Conclusions
Palladium(II) and Platinum(II) Complexes as Synthetic Peptidases / Nebojsa M. Milovic ; Nenad M. KosticChapter 5：
Selective Binding of Metal Complexes to Peptides and Peptide Cleavage
Cleavage of Proteins
Prospects
Acknowledgments
Abbreviations and Symbols
Protease Activity of 1,10-Phenanthroline-Copper Systems / Makoto Kito ; Reiko UradeChapter 6：
Can Free Copper(II) Ions Degrade Proteins?
Protein Degradation by the 1,10-Phenanthroline-Copper(II) Complex
Protease Activity of the Chemically Modified 1,10-Phenanthroline-Copper(II) Complex
Specific Protein Degradation by Copper(II) Ions / Geoffrey AllenChapter 7：
Peptide Sequence Specificity for Cleavage by Copper(II) Ions
Conditions Affecting the Rate of Cleavage of Peptides by Copper(II) Ions
Possible Mechanisms of Copper(II)-Mediated Hydrolysis of Peptide Bonds
Physiological Relevance of the Degradation of Proteins by Copper(II) Ions
Artificial Iron-Dependent Proteases / Saul A. Datwyler ; Claude F. MearesChapter 8：
Introduction: Historical Background and Concepts
Principles and Practical Aspects
Methodology
Transcription Complexes in Escherichia coli
Hydroxyl Radical Footprinting of Proteins Using Metal Ion Complexes / Tomasz Heyduk ; Noel Baichoo ; Ewa HeydukChapter 9：
Experimental Methodology of Protein Footprinting
Applications of Protein Footprinting Methodology
Future Directions
Abbreviations and Definitions
Nickel- and Cobalt-Dependent Oxidation and Cross-Linking of Proteins / Steven E. Rokita ; Cynthia J. BurrowsChapter 10：
Determinants of Nickel- and Cobalt-Dependent Oxidation
Intrinsic Sensitivity of Native Proteins
Mapping Tertiary and Quaternary Structure of Proteins
Effects of Metal Ions on the Oxidation and Nitrosation of Cysteine Residues in Proteins and Enzymes / Ann M. English ; Dean E. WilcoxChapter 11：
Background: Properties and Biological Roles of Cysteine Residues
Oxidation of Cysteines
Nitrosation of Cysteines
Protein Cross-Linking Mediated by Metal Ion Complexes / Kathlynn C. Brown ; Thomas KodadekChapter 12：
Small-Molecule Cross-Linking Reagents Used Free in Solution
Development of Affinity Cross-Linking Reagents: Use of Peptides or Proteins to Deliver a Cross-Linking Reagent Site-Specifically
Ferrocenoyl Amino Acids and Peptides: Probing Peptide Structure / Heinz-Bernhard Kraatz ; Marek GalkaChapter 13：
Introduction: Organometallic Probes in Biological Systems
Synthetic Studies of Ferrocenoyl Amino Acids and Peptides
Structural and Theoretical Studies
Electrochemistry of Ferrocenoyl Amino Acids and Peptides
Summary
Synthetic Analogs of Zinc Enzymes / Gerard ParkinChapter 14：
Structural and Functional Models of Zinc Enzymes as Classified by Active Site Composition
Use of Metal Ion Substitution to Provide Insight into the Structures and Mechanisms of Action of Zinc Enzymes
Perspectives
Mimicking Biological Electron Transfer and Oxygen Activation Involving Iron and Copper Proteins: A Bio(in)organic Supramolecular Approach / Martinus C. FeitersChapter 15：
Mimics for Iron-Sulfur Proteins
Mimics for Blue Copper Proteins
Cytochrome P450 Mimics
Mimics for Oxygen Binding and Activation by Copper Proteins
Concluding Remarks
Subject Index
Preface to the Series
Preface to Volume 38
Contributors
7.

図書
図書
7. Biogeochemistry, availability, and transport of metals in the environment (: hardcover)
edited by Astrid Sigel, Helmut Sigel and Roland K.O. Sigel
出版情報: Boca Raton, Fla. : Taylor & Francis, 2005  xlv, 298 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 44
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8.

図書
図書
8. Inorganic drugs in deficiency and disease
edited by Helmut Sigel with Astrid Sigel
出版情報: New York : M. Dekker, c1982  xxi, 360 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 14
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9.

図書
図書
9. Applications of nuclear magnetic resonance to paramagnetic species
Sigel, Helmut
出版情報: New York : Marcel Dekker, c1987  xxv, 295 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 21
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目次情報: 続きを見る
Preface to the Series
Preface to Volume 21
Contributors
Contents of Other Volumes
Nuclear Relaxation Times as a Source of Structural Information / Gil Navon ; Gianni ValensinChapter 1：
Theoretical Considerations / 1.：
Applications / 2.：
Abbreviations
References
Nuclear Relaxation in NMR of Paramagnetic Systems / Ivano Bertini ; Claudio Luchinat ; Luigi MessoriChapter 2：
Nuclear Relaxation and Observability of the NMR Signals
Physical Consequences of Unpaired Electron-Nucleus Coupling
T[superscript -1 subscript 1M] and Nuclear Magnetic Relaxation Dispersion (NMRD) / 3.：
T[superscript -1 subscript 2M] / 4.：
Electron Relaxation Mechanisms / 5.：
Electron and Nuclear Relaxation in Magnetically Coupled Systems / 6.：
Concluding Remarks / 7.：
NMR Studies of Magnetically Coupled Metalloproteins / Lawrence Que, Jr. ; Michael J. MaroneyChapter 3：
Introduction
Physical Background
Superoxide Dismutase
Hemerythrin
Ribonucleotide Reductase
Uteroferrin
Ferredoxins
Summary / 8.：
Proton NMR Studies of Biological Problems Involving Paramagnetic Heme Proteins / James D. SatterleeChapter 4：
Heme Proteins
The Hyperfine Shift in Paramagnetic Heme Proteins
Resonances of the Porphyrin Ring
Resonances of Axial Ligands
Resonances of the Heme Pocket not Attributable to Heme Ligands
Proton NMR Studies of Protein-Protein Complexes
Conclusion
Metal-Porphyrin Induced NMR Dipolar Shifts and Their Use in Conformational Analysis / Nigel J. Clayden ; Geoffrey R. Moore ; Glyn WilliamsChapter 5：
Theory
Structural and Magnetic Properties of Metalloporphyrins
Conformational Analysis
Conclusions and Outlook
Relaxometry of Paramagnetic Ions in Tissue / Seymour H. Koenig ; Rodney D. Brown IIIChapter 6：
General Background
Relaxometry of Fe[superscript 3+]
Relaxometry of Mn[superscript 2+]
Relaxometry of Gd[superscript 3+]
The Present and Future
Author Index
Subject Index
Preface to the Series
Preface to Volume 21
Contributors
10.

図書
図書
10. ENDOR, EPR, and electron spin echo for probing coordination spheres
Sigel, Helmut
出版情報: New York : Marcel Dekker, c1987  xxiii, 290 p. ; 24 cm
シリーズ名: Metal ions in biological systems / edited by Helmut Sigel ; v. 22
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