Handbook on Metalloproteins

by Bertini; Ivano

• ISBN13: 9780824705206
• ISBN10: 0824705203
• Format: Hardcover
• Copyright: 2001-06-29
• Publisher: CRC Press

Summary

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.

Table of Contents

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	1	(8)
Ivano Bertini
Astrid Sigel
Helmut Sigel
Scope of the Handbook	1	(2)
Organization of the Handbook	3	(1)
Some Web Sites for Further Information	4	(1)
General Comments and Outlook	5	(4)
References	6	(3)
Interaction of Sodium and Potassium with Proteins	9	(30)
Todd M. Larsen
George H. Reed
Introduction	10	(1)
Bioinorganic Chemistry of Na+ and K+	10	(1)
Coordination Chemistry of Na+ and K+	10	(1)
Enzymes/Proteins with Known Structure	11	(4)
Enzymes/Proteins with Unknown Structure	15	(1)
Structure-Function Relationships	15	(16)
Dialkylglycine Decarboxylase	15	(1)
Pyruvate Kinase	16	(3)
Diol Dehydratase	19	(1)
Hsc70	20	(2)
Class II Fructose-1,6-Bisphosphate Aldolase	22	(1)
Fructose-1,6-Bisphosphatase	23	(1)
Carbamoyl Phosphate Synthetase	23	(1)
Cytochrome P450cam	24	(1)
S-Adenosylmethionine Synthetase	24	(1)
Tryptophan Synthase α2β2 Complex	25	(1)
Tryptophanase	26	(2)
Tyrosine Phenol-Lyase	28	(1)
Ascorbate Peroxidase	28	(1)
Methionine Aminopeptidase	29	(1)
Thrombin	30	(1)
α-Amylase	30	(1)
Perspectives	31	(8)
Acknowledgments	32	(1)
Abbreviations and Definitions	32	(1)
References	32	(7)
Structure and Function of Sodium and Potassium Channel Proteins in Membranes	39	(20)
Bernd Fakler
Introduction	40	(1)
Ion Channels: Definition and Role in Excitable Membranes	40	(1)
How Do Voltage-Gated Ion Channels Work?	40	(1)
Potassium and Sodium Channel Proteins with Known Primary Structure	41	(4)
Potassium Channels	42	(2)
Sodium Channels	44	(1)
Structures of Channel Proteins and Protein Domains Resolved to Date	45	(3)
The Pore of a Bacterial Potassium Channel	45	(2)
Inactivation Domains of Mammalian Potassium and Sodium Channels	47	(1)
Structure-Function Relationships	48	(5)
Selectivity and Permeation	48	(2)
Gating: Activation and Inactivation	50	(3)
Perspectives	53	(6)
Acknowledgments	53	(1)
Abbreviations and Definitions	54	(1)
References	54	(5)
Magnesium-Activated Enzyme Systems	59	(34)
Allan Matte
Louis T. J. Delbaere
Introduction	60	(4)
Chemistry of Magnesium	60	(1)
Magnesium-Ligand Chemistry	61	(1)
Metabolism of Magnesium within Prokaryotic and Eukaryotic Cells	62	(2)
Known Structures in Magnesium-Activated Enzyme Systems	64	(8)
Bi-Mg2+-Bound Structures	71	(1)
Kinases	71	(1)
Mg2+-Induced Conformational Changes in Proteins	72	(1)
Unknown Structures	72	(2)
Magnesium-Protoporphyrin IX Chelatase	72	(1)
Sphingomyelinase	73	(1)
Mycobacterial GDP-Mannose Pyrophosphorylase	73	(1)
N1-(5'-Phosphoribosyl)adenosine-5'-monophosphate Cyclohydrolase	73	(1)
Structure-Function Relationships	74	(8)
Kinases	74	(3)
DNA Polymerases	77	(1)
p21ras	78	(1)
Ribozymes	79	(1)
Isocitrate Dehydrogenase	80	(1)
Xylose Isomerase	81	(1)
Conclusions	82	(11)
Acknowledgments	82	(1)
Abbreviations	82	(2)
References	84	(9)
Calcium and Its Enzymes	93	(60)
Andreas Muranyi
Bryan E. Finn
Introduction	94	(6)
Aims and Scope	94	(1)
Coordination Chemistry of Ca2+	95	(1)
Bioinorganic Role of Ca2+	95	(1)
Homeostasis and Metabolism	95	(2)
Distribution of Ca2+-Binding Proteins	97	(2)
Introduction to Systems Chosen for Discussion	99	(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