Metal carbon bonds in enzymes and cofactors:
Saved in:
| Format: | Book |
|---|---|
| Language: | English |
| Published: |
Cambridge
RSC Publ.
2009
|
| Series: | Metal ions in life sciences
6 |
| Subjects: | |
| Online Access: | Inhaltsverzeichnis |
| Physical Description: | XXVII, 510 S. Ill., graph. Darst. |
| ISBN: | 9781847559159 |
Staff View
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Record in the Search Index
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|---|---|
| adam_text | Titel: Metal carbon bonds in enzymes and cofactors
Autor: Sigel, Astrid
Jahr: 2009
Contents
HISTORICAL DEVELOPMENT
AND PERSPECTIVES OF THE SERIES v
PREFACE TO VOLUME 6 vii
CONTRIBUTORS TO VOLUME 6 xvii
TITLES OF VOLUMES 1-44 IN THE
METAL IONS IN BIOLOGICAL SYSTEMS SERIES xix
CONTENTS OF VOLUMES IN THE
METAL IONS IN LIFE SCIENCES SERIES xxi
1 ORGANOMETALLIC CHEMISTRY OF B12 COENZYMES 1
Bernhard Krautler
Abstract 2
1. Introduction 2
2. Structure of Bi2 Derivatives in the Crystal and in Solution 5
3. Redox Chemistry of B12 Derivatives 18
4. Reactivity of B,2 Derivatives in Organometallic Reactions 24
5. Organometallic Bl2 Derivatives as Cofactors and
Intermediates in Enzymes 34
6. Concluding Remarks and Future Directions 40
Acknowledgments 41
Abbreviations 41
References 42
Mcud Ions in Lite Svwnci s. Volume 6 Edited b Astrid Sigel. Helmut Sigd. and Roland K. (). Stgel
« Ro al Society of Chemistr :009
Published by the Royal Society of Chemistry, vvuw.rsc.org DOI: 1(1.1019 97K1S4755S) 1 59-FP01 I
xii CONTENTS
2 COBALAMIN- AND CORRINOID-DEPENDENT
ENZYMES 53
Rowena G. Matthews
Abstract 54
1. Introduction. What Is a Corrinoid? 54
2. Corrinoid-Dependent Methyltransferases 56
3. Adenosylcobalamin-Dependent Rearrangements and
Eliminations 84
4. Concluding Remarks 106
Acknowledgments 107
Abbreviations and Definitions 107
References 107
3 NICKEL-ALKYL BOND FORMATION IN THE ACTIVE
SITE OF METHYL-COENZYME M REDUCTASE 115
Bernhard Jaun and Rudolf K. Thauer
Abstract 116
1. Introduction 116
2. Nickel-Carbon Bond Formation in Free Coenzyme F430 119
3. Nickel-Alkyl Bond Formation in MCR Upon Inactivation
with Alkyl Halides 120
4. Methyl-Nickel Bond Formation in Methyl-Coenzyme M
Reductase During Catalysis? 123
5. Observations to Be Followed Up 129
Acknowledgments 129
Abbreviations 129
References 130
4 NICKEL-CARBON BONDS IN ACETYL-COENZYME A
SYNTHASES/CARBON MONOXIDE
DEHYDROGENASES 133
Paid A. Lindahl
Abstract 133
1. Introduction 134
2. Redox and Catalytic Properties of the A- and
C-Clusters 137
3. Evidence for a Ni-CO Bond in the Ared-CO State of the
A-cluster 139
CONTENTS xiii
4. Evidence for a Ni-CH3 Bond in the Methylated Intermediate
of the A-Cluster 139
5. Evidence for a Ni-C(O)CH3 Bond in the Acetyl Intermediate
of the A-Cluster 140
6. Evidence for a Ni-CO Bond in the C-Cluster 141
7. Evidence for a Ni-C(O)O-Fe Bond in
the C-Cluster 143
8. Conclusions and Future Studies 144
Acknowledgment 147
Abbreviations and Definitions 147
References 147
5 STRUCTURE AND FUNCTION OF [NiFe]-HYDRO-
GENASES 151
Juan C. Fontecilla-Camps
Abstract 152
1. Introduction 152
2. Hydrogenase Structure 153
3. Hydrogenase Maturation and Active Site Assembly 160
4. Electron Transfer 165
5. Proton Transfer 166
6. Oxidized Inactive States of the [NiFe]-Hydrogenase Active Site 168
7. Substrate Binding and Catalysis 172
8. Concluding Remarks 173
Acknowledgments 173
Abbreviations 173
References 174
6 CARBON MONOXIDE AND CYANIDE LIGANDS IN THE
ACTIVE SITE OF [FeFe]-HYDROGENASES 179
John W. Peters
Abstract 180
1. Introduction 180
2. [FeFe]-Hydrogenase Structure 181
3. [FeFe]-Hydrogenase Spectroscopic Studies 192
4. H-Cluster Model Complexes 195
5. H-Cluster Biosynthesis 199
6. Future Directions 206
Acknowledgments 207
xiv CONTENTS
Abbreviations and Definitions 208
References 208
7 CARBON MONOXIDE AS INTRINSIC LIGAND TO IRON
IN THE ACTIVE SITE OF [Fe]-HYDROGENASE 219
Seigo Shima, Rudolf K. Thauer, and Ulrich Ermler
Abstract 220
1. Introduction 220
2. Physiology 222
3. The Iron Guanylylpyridinol Cofactor in the Enzyme-Free
State 223
4. Structure of [Fe]-Hydrogenase with and without the Iron
Guanylylpyridinol Cofactor Bound 227
5. Ligands to Iron in the Active Site of [Fe]-Hydrogenase 231
6. Proposed Catalytic Mechanisms 235
7. Concluding Remarks 237
Acknowledgments 237
Abbreviations 237
References 238
8 THE DUAL ROLE OF HEME AS COFACTOR AND
SUBSTRATE IN THE BIOSYNTHESIS OF CARBON
MONOXIDE 241
Mario Rivera and Juan C. Rodriguez
Abstract 242
1. Introduction 243
2. The Biosynthesis of Carbon Monoxide 247
3. Heme Oxygenase Favors Heme Hydroxylation over
Ferryl Formation. The Nature of the Ferric Hydroperoxide
Complex in Heme Oxygenase 259
4. Heme Oxygenase Dynamics and Heme Breakdown. The
Distal Ligand Has a Profound Effect in the Dynamic
Behavior of Heme Oxygenase 268
5. The Regioselectivity of Heme Hydroxylation 276
6. Conclusion and Outlook 284
Acknowledgments 285
Abbreviations 286
References 286
CONTENTS xv
9 COPPER-CARBON BONDS IN MECHANISTIC AND
STRUCTURAL PROBING OF PROTEINS AS WELL AS
IN SITUATIONS WHERE COPPER IS A CATALYTIC
OR RECEPTOR SITE 295
Heather R. Lucas and Kenneth D. Karlin
Abstract 296
1. Introduction 297
2. Binuclear Copper Proteins 298
3. Heterobimetallic Copper-Containing Enzymes 317
4. Non-Blue Copper Oxidases 334
5. Blue, Green, and Purple Copper Proteins 337
6. Copper(I) Recognition Sites or Receptors 344
7. Miscellaneous 346
8. General Conclusions 349
Acknowledgments 350
Abbreviations 351
References 352
10 INTERACTION OF CYANIDE WITH ENZYMES
CONTAINING VANADIUM, MANGANESE,
NON-HEME IRON, AND ZINC 363
Martha E. Sosa- Torres and Peter M. H. Kroneck
Abstract 364
1. Introduction 364
2. Vanadium Enzymes 368
3. Manganese Enzymes 373
4. Non-Heme Iron Enzymes 377
5. Zinc Enzymes 383
6. Conclusions 388
Acknowledgments 388
Abbreviations 388
References 389
11 THE REACTION MECHANISM OF THE MOLYBDENUM
HYDROXYLASE XANTHINE OXIDOREDUCTASE:
EVIDENCE AGAINST THE FORMATION OF
INTERMEDIATES HAVING METAL-CARBON BONDS 395
Russ Hille
Abstract 396
1. Introduction 396
xvi CONTENTS
2. Electron-Nuclear Double Resonance Studies of the
Very Rapid Species 400
3. X-Ray Crystal Structures Relevant to The Reaction
Mechanism 404
4. General Conclusions 413
Acknowledgments 414
Abbreviations and Definitions 414
References 414
12 COMPUTATIONAL STUDIES OF BIOORGANOMETALLIC
ENZYMES AND COFACTORS 417
Matthew D. Liptak, Katherine M. Van Heuvelen, and
Thomas C. Brunold
Abstract 418
1. Introduction 419
2. Computational Approaches to Bioorganometallic
Chemistry 420
3. Formation and Cleavage of the Co-C Bond of Cobalamin
in Enzyme Active Sites 426
4. Organometallic Chemistry and Catalytic Cycle of
Methyl-Coenzyme M Reductase 435
5. Geometric and Electronic Structures of the Carbon
Monoxide Dehydrogenase/Acetyl-Coenzyme A Synthase
Active Site Clusters 442
6. Magnetic Properties of the Active Site Cluster of Iron-Only
Hydrogenases 447
7. Concluding Remarks and Future Directions 450
Acknowledgments 452
Abbreviations 452
References 454
SUBJECT INDEX 461
AUTHOR INDEX OF CONTRIBUTORS TO MIBS-X TO
MIBS-44 AND MILSA TO MILS-6 497
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| spelling | Metal carbon bonds in enzymes and cofactors ed. by Astrid Sigel ... Cambridge RSC Publ. 2009 XXVII, 510 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Metal ions in life sciences 6 Coenzymes Coenzymes chemistry Metalloenzymes Multienzyme Complexes chemistry Organometallic Compounds chemistry Organometallic compounds Oxidoreductases chemistry Vitamin B 12 chemistry Vitamin B12 Cofaktor (DE-588)4343425-3 gnd rswk-swf Enzym (DE-588)4014988-2 gnd rswk-swf Metallorganische Verbindungen (DE-588)4038906-6 gnd rswk-swf Metallorganische Verbindungen (DE-588)4038906-6 s Enzym (DE-588)4014988-2 s Cofaktor (DE-588)4343425-3 s DE-604 Sigel, Astrid Sonstige (DE-588)103367866X oth Metal ions in life sciences 6 (DE-604)BV022275400 6 HBZ Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=017618346&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Metal carbon bonds in enzymes and cofactors Metal ions in life sciences Coenzymes Coenzymes chemistry Metalloenzymes Multienzyme Complexes chemistry Organometallic Compounds chemistry Organometallic compounds Oxidoreductases chemistry Vitamin B 12 chemistry Vitamin B12 Cofaktor (DE-588)4343425-3 gnd Enzym (DE-588)4014988-2 gnd Metallorganische Verbindungen (DE-588)4038906-6 gnd |
| subject_GND | (DE-588)4343425-3 (DE-588)4014988-2 (DE-588)4038906-6 |
| title | Metal carbon bonds in enzymes and cofactors |
| title_auth | Metal carbon bonds in enzymes and cofactors |
| title_exact_search | Metal carbon bonds in enzymes and cofactors |
| title_full | Metal carbon bonds in enzymes and cofactors ed. by Astrid Sigel ... |
| title_fullStr | Metal carbon bonds in enzymes and cofactors ed. by Astrid Sigel ... |
| title_full_unstemmed | Metal carbon bonds in enzymes and cofactors ed. by Astrid Sigel ... |
| title_short | Metal carbon bonds in enzymes and cofactors |
| title_sort | metal carbon bonds in enzymes and cofactors |
| topic | Coenzymes Coenzymes chemistry Metalloenzymes Multienzyme Complexes chemistry Organometallic Compounds chemistry Organometallic compounds Oxidoreductases chemistry Vitamin B 12 chemistry Vitamin B12 Cofaktor (DE-588)4343425-3 gnd Enzym (DE-588)4014988-2 gnd Metallorganische Verbindungen (DE-588)4038906-6 gnd |
| topic_facet | Coenzymes Coenzymes chemistry Metalloenzymes Multienzyme Complexes chemistry Organometallic Compounds chemistry Organometallic compounds Oxidoreductases chemistry Vitamin B 12 chemistry Vitamin B12 Cofaktor Enzym Metallorganische Verbindungen |
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