Bioinspired catalysis: metal-sulfur complexes
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| Sprache: | English |
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Weinheim
Wiley-VCH
2015
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| Beschreibung: | XVIII, 417 S. Ill., graph. Darst. |
| ISBN: | 3527333088 9783527333080 9783527664160 |
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CONTENTS
LIST OF CONTRIBUTORS
XIII
PREFACE '
XVII
PART I PRIMORDIAL METAL-SULFUR-MEDIATED REACTIONS 1
1 FROM CHEMICAL INVARIANCE
TO GENETIC VARIABILITY 3
GUNTER
WACHTERSHAUSER
1.1 , HEURISTIC OF BIOCHEMICAL RETRODICTION 3
1.2 RETRODICTING THE ELEMENTS OF LIFE 5
1.3 RETRODICTING PIONEER CATALYSIS 6
1.4 RETRODICTING METABOLIC REPRODUCTION AND EVOLUTION 10
1.5 RETRODICTING PIONEER-METABOLIC REACTIONS 11
1.6 EARLY EVOLUTION IN A
SPATIOTEMPORAL FLOW CONTEXT 13
ACKNOWLEDGMENTS 16
REFERENCES 16
2
FE-S CLUSTERS: BIOGENESIS
AND REDOX,
CATALYTIC, AND REGULATORY
PROPERTIES 21
YVAIN NICOLET AND
JUAN
C. FONTECILLA-CAMPS
2.1 INTRODUCTION 21
2.2 FE-S CLUSTER BIOGENESIS AND TRAFFICKING 22
2.3 REDOX PROPERTIES OF FE-S CLUSTERS 27
2.4 FE-S CLUSTERS AND CATALYSIS 28
2.4.1 REDOX CATALYSIS 28
2.4.2 NONREDOX FE-S CLUSTER-BASED CATALYSIS 30
2.5 FE-S CLUSTERS AND OXIDATIVE STRESS 32
2.6 REGULATION OF PROTEIN EXPRESSION BY^ FE - S CLUSTERS 33
2.6.1 EUKARYOTIC IRON REGULATORY PROTEIN 1 (IRP1) 34
2.6.1.1 IRP1 AND FE-S CLUSTER BIOGENESIS 35
2.6.1.2 REACTIVE OXYGEN SPECIES AND IRP1 FE-S CLUSTER
STABILITY 35
2.6.1.3 X-RAY STRUCTURAL STUDIES OF IRP1
- IRE COMPLEXES 36
2.6.2 BACTERIAL FUMARATE NITRATE REDUCTION REGULATOR (FNR) 37
HTTP://D-NB.INFO/1050181085
VII CONTENTS
2.6.3 THE ISC ASSEMBLY MACHINERY REGULATOR ISCR 38
2.7 CONCLUSION 38
REFERENCES 39
PART II MODEL COMPLEXES
OF THE ACTIVE
SITE
OF HYDROGENASES -
PROTON AND DIHYDROGEN ACTIVATION
49
3
[NIFE] HYDROGENASES
SI
JOE DAWSON,
CARLO PEROTTO,
JONATHAN MCMASTER,
AND MARTIN SCHRODER
3.1 INTRODUCTION 51
3.2 INTRODUCTION TO [NIFE] HYDROGENASES 52
3.3 NICKEL THIOLATE COMPLEXES AS ANALOGS OF [NIFE] HYDROGENASE 52
3.4 [NIFE] HYDROGENASE MODEL COMPLEXES 59
3.4.1 AMINE [N
2
NI(JI-S
2
)FE] COMPLEXES 59
3.4.2 PHOSPHINE [P
2
NI((J-S
2
)FE] COMPLEXES 60
3.4.3 THIOLATE [S
X
NI(|I-S
Y
)FE]
COMPLEXES 63
3.4.4 POLYMETALLIC [NI(|I-S)
2
FE^] COMPLEXES 65
3.5 ANALOGS OF [NIFE] HYDROGENASE INCORPORATING PROTON RELAYS 67
3.5.1 NICKEL COMPLEXES INCORPORATING PROTONATION SITES 68
3.5.2 [NIFE] COMPLEXES'INCORPORATING PROTONATION SITES 72
3.6 PERSPECTIVES AND FUTURE CHALLENGES 74
ACKNOWLEDGMENTS 74
REFERENCES 74
4 [FEFE] HYDROGENASE MODELS:
AN OVERVIEW 79
ULF-PETERAPFEL, FRANQOIS
Y. PETITION,
PHILIPPE SCHOLIHAMMER,
JEAN TAIARMIN,
AND WOLFGANG
WEIGAND
4.1 INTRODUCTION 79
4.2 SYNTHETIC STRATEGIES TOWARD [FEFE] HYDROGENASE MODEL
COMPLEXES 81
4.3 PROPERTIES OF MODEL COMPLEXES 83
4.3.1 BIOMIMETIC MODELS OF THE "ROTATED STATE" 83
4.3.2 ELECTRON TRANSFER IN [FEFE] HYDROGENASE MODELS 84
4.3.3 PROTONATION CHEMISTRY OF [FEFE] HYDROGENASE MODELS 86
4.3.3.1 HYDRIDE FORMATION 86
4.3.3.2 LIGAND PROTONATION AND PROTON RELAYS 88
4.3.4 WAFER-SOLUBLE HYDROGENASE MIMICS 94
4.4 CONCLUSION 96
REFERENCES 96 ~ - .
5 THE
THIRD HYDROGENASE 105
CALLUM SCULLION
AND JOHN
A. MURPHY
5.1 INTRODUCTION
10S
5.2 INITIAL STUDIES OF HMD 106
5.3 DISCOVERY THAT HMD CONTAINS A BOUND CO FACTOR 109
CONTENTS IVII
5.4 DISCOVERY THAT HMD IS A METALLOENZYME 109
5.5 CRYSTAL STRUCTURE STUDIES OF [FE] HYDROGENASE 111
5.6 MECHANISTIC MODELS OF [FE] HYDROGENASE 118
5.6.1 STUDIES BEFORE THE MOST RECENT ASSIGNMENT OF THE FEGP
COFACTOR 118 *:
5.6.2 STUDIES AFTER THE MOST RECENT ASSIGNMENT OF THE FEGP
COFACTOR 120
5.6.3 SYNTHESIZED MODEL COMPLEXES OF THE FEGP COFACTOR 126
REFERENCES 134
6 DFT INVESTIGATION OF MODELS RELATED TO THE ACTIVE SITE
OF HYDROGENASES 137
CLAUDIO
GRECO AND LUCA DE GIOIA
6.1 INTRODUCTION 137
6.2 QM STUDIES OF HYDROGENASES 138
6.3 QM STUDIES OF SYNTHETIC COMPLEXES RELATED TO THE ACTIVE SITE
OF HYDROGENASES 145
6.3.1 DFT STUDIES ABOUT STRUCTURAL AND REDOX PROPERTIES OF SYNTHETIC
COMPLEXES RELATED TO THE ACTIVE SITE OF [FEFE] HYDROGENASES 146
6.3.2 DFT STUDIES ABOUT THE REACTIVITY OF SYNTHETIC MODELS RELATED TO
THE
ACTIVE SITE OF [FEFE] HYDROGENASES 149
6.3.3 DFT STUDIES ABOUT REGIOCHEMISTRY OF PROTONATION OF SYNTHETIC
I COMPLEXES RELATED TO THE ACTIVE SITE OF [FEFE] HYDROGENASES 152
6.3.4 DFT STUDIES ABOUT THE ISOMERIZATION OF SYNTHETIC COMPLEXES RELATED
TO THE ACTIVE SITE OF [FEFE] HYDROGENASES 154
6.4 CONCLUSIONS 156
REFERENCES 156
7 MECHANISTIC ASPECTS
OF BIOLOGICAL HYDROGEN EVOLUTION AND
UPTAKE 161
JOSEPH A. WRIGHT AND
CHRISTOPHER J. PICKETT
7.1 INTRODUCTION 161
7.2 [FEFE] HYDROGENASES 161
7.2.1 OVERVIEW OF THE CATALYTIC CYCLE 161
7.2.2 THE NATURE OF THE BRIDGEHEAD ATOM 163
7.2.3 STRUCTURAL FEATURES OF THE RESTING STATE (H
OX
) AND REDUCED STATE
(FIRED) F TH
E
ACTIVE SITE 164
7.2.4 RELATIONSHIP BETWEEN STRUCTURAL AND SPECTROSCOPIC PROPERTIES OF
H
OX
. ^RED
AN
D H
SRED
164 *
7.2.5 THE ROTATED STATE AND MIXED VALENCY: SYNTHETIC SYSTEMS 167
7.2.6 HYDRIDES 170
7.2.7 HYDRIDES AND ELECTROCATALYSIS OF HYDROGEN EVOLUTION 174
7.2.8 DIHYDROGEN OXIDATION 177
7.2.9 FINAL COMMENTS 180
7.3 [NIFE] HYDROGENASES 180
VIII
| CONTENTS
7.3.1 OVERVIEW OF THE CATALYTIC CYCLE 180
7.3.2 STRUCTURAL MODELS OF NI-A, NI-B, AND NI-SI STATES 182
7.3.3 HYDRIDE CHEMISTRY RELATED TO NI-C/NI-R: FUNCTIONAL MODELS 183
7.3.4 FINAL COMMENTS 186
7.4 [FE] HYDROGENASE 186
7.4.1 OVERVIEW 186
7.4.2 BIOLOGICAL MECHANISM 187
7.4.3 MODEL STUDIES 189
7.4.4 FINAL COMMENTS 191
7.5 NITROGENASE 191
7.5.1 OVERVIEW 191
7.5.2 HYDROGEN EVOLUTION BY MO-NITROGENASE 192
7.5.3 PARAMAGNETIC BRIDGING FE/FE HYDRIDES 193
7.5.4 FINAL COMMENTS 194
REFERENCES 194
PART III NITROGEN FIXATION 199
8 STRUCTURES AND FUNCTIONS OF THE ACTIVE
SITES OF NITROGENASES 201
CHICHUNGLEE,JAREDA. WIIG,
YILINHU,ANDMARKUSW.RIBBE
8.1 INTRODUCTION 201
8.2 PROPERTIES OF MO NITROGENASE 202
8.2.1 PROPERTIES OF FE PROTEIN AND ITS ASSOCIATED CLUSTER 202
8.2.1.1 THE FE PROTEIN STRUCTURE 202
8.2.1.2 THE [FE
4
S
4
] CLUSTER 204
8.2.2 PROPERTIES OF MOFE PROTEIN AND ITS ASSOCIATED CLUSTERS 204
8.2.2.1 THE MOFE PROTEIN 204
8.2.2.2 THE P-CLUSTER 204
8.2.2.3 THE FEMO-CO 206
8.3 CATALYSIS BY MO NITROGENASE 206
8.3.1 THE THORNELEY-LOWE MODEL 207
8.3.1.1 THE FE PROTEIN CYCLE 207
8.3.1.2 THE MOFE PROTEIN CYCLE 208
8.3.2 RECENT DEVELOPMENT 210
8.3.2.1 ALTERNATIVE PATHWAY OF N
2
REDUCTION 210
8.3.2.2 PLAUSIBLE STRUCTURES OF N
2
REDUCTION INTERMEDIATES 210
8.3.2.3 ALTERNATIVE SUBSTRATES OF NITROGENASE 211
8.4 UNIQUE FEATURES OF V NITROGENASE 213
8.4.1 STRUCTURAL FEATURES OF FE PROTEIN AND ITS ASSOCIATED CLUSTER 213
8.4.1.1 THE FE PROTEIN 213
8.4.1.2 THE [FE
4
S
4
] CLUSTER 214
8.4.2 STRUCTURAL FEATURES OFVFE PROTEIN AND ITS ASSOCIATED CLUSTERS 214
8.4.2.1 THE VFE PROTEIN 214
8.4.2.2 THE P-CLUSTER OFVFE PROTEIN 215
8.4.2.3 THE FEVCO 216
CONTENTS IX
8.4.3 CATALYTIC FEATURES OF VNITROGENASE 217
8.5 CATALYTIC PROPERTIES OF ISOLATED FEMO-CO AND FEVCO 220
ACKNOWLEDGMENTS 221
REFERENCES 221
9 MODEL COMPLEXES
OF THE ACTIVE
SITE OF NITROGENASES: RECENT
ADVANCES 225
FR6D6RIC BARRIERE
9.1 INTRODUCTION 225
9.2 STRUCTURAL MODELS OF METAL - SULFUR CLUSTERS IN THE
NITROGENASES 227
9.3 FUNCTIONAL MODELING AT A SINGLE MOLYBDENUM CENTER 229
9.4 FUNCTIONAL MODELING AT A SINGLE IRON CENTER 231
9.5 THE HYDROGEN AND HOMOCITRATE ISSUES IN NITROGENASE MODEL
CHEMISTRY 235
9.6 SULFUR- AND METAL-METAL INTERACTION IN FUNCTIONAL MODELS OF
NITROGENASE 238
9.7 SURFACE CHEMISTRY AND THE SUPRAMOLECULAR PROTEIN
ENVIRONMENT 242
9.8 CONCLUSION AND OUTLOOK 243
REFERENCES 245
10 A UNIFIED CHEMICAL MECHANISM FOR HYDROGENATION REACTIONS
CATALYZED BY NITROGENASE 249
IAN DANCE
10.1 INTRODUCTION 249
10.1.1 NITROGENASE: THE ENZYME 249
10.1.2 FEMO-CO 250
10.1.3 WHERE DOES THE CATALYSIS OCCUR ON FEMO-CO? 251
10.2 INVESTIGATIONS OF MECHANISM 251
10.2.1 DENSITY FUNCTIONAL SIMULATIONS 252
10.2.2 THE COORDINATION CHEMISTRY OF FEMO-CO 253
10.2.3 ELECTRONIC STRUCTURE OF FEMO-CO 254
10.3 HYDROGEN SUPPLY FOR THE REACTIONS OF NITROGENASE 254
10.3.1 MULTIPLE PROTONS ARE NEEDED FOR CATALYTIC REACTION CYCLES 254
10.3.2 THE PROTON SUPPLY CHAIN 255
10.3.3 HYDROGENATION OF FEMO-CO 256
10.3.4 HYDROGEN ATOM MIGRATION OVER FEMO-CO 257
10.4 FEMO-CO IN NITROGENASE AS AGENERAL HYDROGENATING MACHINE 259
10.4.1 MODES OF SUBSTRATE BINDING TO FEMO-CO 259
10.4.2 VECTORIAL HYDROGENATION OF FEMO-CO IN RELATION TO SUBSTRATE
BINDING 260
10.4.3 THE INTRAMOLECULAR HYDROGENATION PARADIGM FOR THE CATALYTIC
REACTIVITY OF FEMO-CO 261
X | CONTENTS
10.5 CHEMICAL MECHANISMS FOR THE CATALYSIS OF SUBSTRATE HYDROGENATION
AT FEMO-CO 263
10.5.1 HOW DOES N
2
BOND TO FEMO-CO? 263
10.5.2 PROPOSED INTIMATE CHEMICAL MECHANISM FOR THE CATALYSIS OF
HYDROGENATION OF N
2
TO NH
3
AT FEMO-CO 264
10.5.2.1 POSSIBILITIES 264
10.5.2.2 PRELIMINARY SIMULATIONS 264
10.5.2.3 COMPLETE 21-STEP CHOREOGRAPHY 265
10.6 HYDROGEN TUNNELING IN THE NITROGENASE MECHANISM 267
10.6.1 CHARACTERISTICS OF H ATOM TUNNELING IN ENZYME REACTIONS 267
10.6.2 CHARACTERISTICS OF H-ATOM TRANSFER IN NITROGENASE 268
10.7 INTRAMOLECULAR HYDROGENATION OF OTHER SUBSTRATES 270
10.7.1 FORMATION OF DIHYDROGEN 270
10.7.2 HYDROGENATION OF ALKYNES 270
10.7.3 HYDROGENATION OF D
2
: THE HD REACTION 273
10.7.4 HYDROGENATION OF CO AND C0
2
273
10.8 INTERPRETATION OF THE STRUCTURE OF FEMO-CO AND ITS SURROUNDS 277
10.9 MIMICKING NITROGENASE 278
10.10 SUMMARY AND EPILOG 279
ACKNOWLEDGMENTS 280
REFERENCES 280
11 BINDING SUBSTRATES TO SYNTHETIC FE-S-BASED CLUSTERS AND THE POSSIBLE
RELEVANCE TO NITROGENASES 289
RICHARD A. HENDERSON
11.1 INTRODUCTION 289
11.2 MECHANISM OF NITROGENASES 290
11.2.1 DETECTING SUBSTRATES AND INTERMEDIATES BOUND TO THE ENZYME 292
11.2.2 EXPLORING INTERMEDIATES IN THE ENZYME MECHANISM USING
CALCULATIONS 294
11.3 STUDIES ON SYNTHETIC CLUSTERS 296
11.3.1 EVIDENCE FOR
SUBSTRATES BOUND TO SYNTHETIC CLUSTERS 296
11.3.2 MECHANISMS OF SUBSTRATES BINDING TO FE-S-BASED CLUSTERS 299
11.3.3 MECHANISMS PECULIAR TO CLUSTERS 303
11.3.4 INFLUENCE OF CLUSTER COMPOSITION ON SUBSTRATE BINDING 304
11.3.5 TRANSIENT BINDING OF SUBSTRATES TO CLUSTERS 305
11.3.5.1 INFLUERFCE OF METAL COMPOSITION ON TRANSIENT BINDING AFFINITIES
OF
SUBSTRATES 309
11.3.5.2 RATES OF BINDING
SUBSTRATES TO CLUSTERS 309
11.3.6 PROTONATION OF CLUSTERS 310
11.3.6.1 KINETICS AND THERMODYNAMICS OF PROTONATION OF CLUSTERS 311
11.3.6.2 TIMING OF BINDING PROTONS AND SUBSTRATES TO CLUSTERS 311
11.3.6.3 THE PROBLEM OF BINDING SUBSTRATE VERSUS REDUCTION
OF PROTONS 313
11.4 STUDIES ON EXTRACTED FEMO-COFACTOR 316
CONTENTS | XI
11.4.1 EVIDENCE FOR SUBSTRATES BINDING TO EXTRACTED FEMO-COFACTOR 316
11.4.2 RATES OF SUBSTRATE BINDING TO EXTRACTED FEMO-COFACTOR 318
11.5 THE FUTURE 320
REFERENCES 321
PART IV MISCELLANEOUS:
CO, RCN ACTIVATION, DMSO REDUCTION
32S
12 SULFUR-OXYGENATION AND FUNCTIONAL MODELS OF NITRILE HYDRATASE 327
DAVINDER KUMAR
AND CRAIG A. GRAPPERHAUS
12.1 INTRODUCTION 327
12.2 NITRILE HYDRATASE 327
12.2.1 SIGNIFICANCE 327
12.2.2 ENZYME ACTIVE SITE 328
12.2.3 REACTION CYCLE 329
12.3 SMALL-MOLECULE MIMICS 330
12.4 EARLY S-OXYGENATION STUDIES 332
12.5 SULFUR-OXYGENATION OF CO(III) NHASE MIMICS 333
12.5.1 N
2
S
2
CO(III)
MODEL COMPLEXES 334
12.5.2 N
3
S
2
CO(III)
MODEL COMPLEXES 335
12.5.3 N
2
S
3
CO(III) MODEL COMPLEXES 337
12.6 SULFUR-OXYGENATION OF FE(III) NHASE MIMICS 339
12.6.1 N
2
S
2
-FE(III) MODEL COMPLEXES 339
12.6.2 N
3
S
2
-FE(III) MODEL COMPLEXES 340
12.6.3 N
2
S
3
FE(III) MODEL COMPLEXES 341
12.7 RUTHENIUM COMPLEXES 343
12.8 CONCLUSIONS/CHALLENGES 344
ABBREVIATIONS 345
REFERENCES 345
13 MOLYBDENUM AND TUNGSTEN OXIDOREDUCTASE MODELS 349
CAROLA SCHULZKE
AND ASHTA
CHANDRA
GHOSH
13.1 INTRODUCTION 349
13.2 CLASSIFICATION OF MOLYBDENUM- AND TUNGSTEN-DEPENDENT
ENZYMES 351
13.3 LIGAND SYSTEMS COMMONLY USED IN MODEL STUDIES 353
13.4 SELECTED MOLYBDENUM-CONTAINING ENZYMES AND RELEVANT MODELING
CHEMISTRY 355
13.4.1 ENZYMES OF THE XANTHINE OXIDASE (XO) FAMILY 355
13.4.1.1 CRYSTAL STRUCTURES AND ACTIVE SITE COMPOSITION OF XO-RELATED
ENZYMES 355
13.4.1.2 MECHANISTIC IMPLICATIONS 356
13.4.1.3 MODEL COMPLEXES FOR THE XANTHINE OXIDASE FAMILY 357
13.4.2 THE SULFITE
OXIDASE (SO) FAMILY 360
13.4.2.1 CRYSTAL STRUCTURES AND ACTIVE SITE COMPOSITION OF SO-FAMILY
ENZYMES 360
XII
| CONTENTS
13.4.2.2 MECHANISTIC IMPLICATIONS 361
13.4.2.3 MODEL COMPLEXES FOR THE SULFITE OXIDASE FAMILY 362
13.4.3 THE DMSO REDUCTASE (DMSOR) FAMILY 365
13.4.3.1 CRYSTAL STRUCTURES AND ACTIVE SITE COMPOSITION OF THE DMSOR
FAMILY ENZYMES 367
13.4.3.2 MECHANISTIC IMPLICATIONS 368
13.4.3.3 MODEL COMPLEXES FOR THE DMSOR FAMILY 369
13.5 SELECTED TUNGSTEN-CONTAINING ENZYMES AND RELEVANT MODEL
CHEMISTRY 372
13.5.1 THE ALDEHYDE FERREDOXIN OXIDOREDUCTASE (AOR) FAMILY 372
13.5.1.1 MODEL CHEMISTRY FOR THE AOR FAMILY 373
13.5.2 THE FORMATE DEHYDROGENASE (FDH) FAMILY OF ENZYMES 375
13.5.2.1 MODEL CHEMISTRY FOR THE W-FDH FAMILY 376
13.5.3 ACETYLENE HYDRATASE 376
REFERENCES 377
PART V APPLICATIVE PERSPECTIVES 383
14 ELECTRODE MATERIALS
AND ARTIFICIAL PHOTOSYNTHETIC SYSTEMS 385
PHONG D. TRAN,
MARC FONTECAVE,
AND VINCENT
ARTERO
14.1 INTRODUCTION 385
14.2 ELECTRODE MATERIALS FOR HYDROGEN EVOLUTION 385
14.2.1 ELECTRODE MATERIALS BASED ON BIO-INSPIRED MOLECULAR CATALYST 386
14.2.1.1 ENTRAPMENT OF CATALYST WITHIN A POLYMERIC MATERIAL 386
14.2.1.2 COVALENT ATTACHMENT OF CATALYST TO ELECTRODE MATERIAL 388
14.2.1.3 NONCOVALENT ATTACHMENT OF CATALYST TO ELECTRODE MATERIAL VIA
N-IT
STACKING INTERACTION 392
14.2.2 ELECTRODE MATERIALS BASED ON BIO-INSPIRED ALL-INORGANIC
CATALYSTS 394
14.2.2.1 METAL-SULFIDE CATALYSTS 394
14.2.2.2 ELECTRODE ENGINEERING FROM METAL-SULFIDE CATALYSTS 395
14.3 PHOTOELECTRODE MATERIALS FOR HYDROGEN EVOLUTION 397
14.3.1 ALL-INORGANIC PHOTOCATALYSTS COMPOSED OF SOLID-STATE
SEMICONDUCTOR AND SOLID INORGANIC CATALYST 397
14.3.2 SOLID-STATE SEMICONDUCTOR AND MOLECULAR CATALYST 399
14.3.3 ALL-MOLECULAR-BASED ELECTRODE MATERIALS 400
14.4 ARTIFICIAL PHOTOSYNTHETIC SYSTEMS 401
14.5 TOWARD PHOTOELECTRODE MATERIALS FOR C0
2
REDUCTION 404
14.6 CONCLUSION AND PERSPECTIVE 406
REFERENCES 407
INDEX
411 |
| any_adam_object | 1 |
| author2 | Weigand, Wolfgang 1958- |
| author2_role | edt |
| author2_variant | w w ww |
| author_GND | (DE-588)1062586395 |
| author_facet | Weigand, Wolfgang 1958- |
| building | Verbundindex |
| bvnumber | BV042082299 |
| classification_rvk | VE 7040 VH 8082 VK 5580 VK 8700 |
| ctrlnum | (OCoLC)878979316 (DE-599)DNB1050181085 |
| dewey-full | 541.395 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 541 - Physical chemistry |
| dewey-raw | 541.395 |
| dewey-search | 541.395 |
| dewey-sort | 3541.395 |
| dewey-tens | 540 - Chemistry and allied sciences |
| discipline | Chemie / Pharmazie |
| format | Book |
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| genre | (DE-588)4143413-4 Aufsatzsammlung gnd-content |
| genre_facet | Aufsatzsammlung |
| id | DE-604.BV042082299 |
| illustrated | Illustrated |
| indexdate | 2024-12-20T11:02:17Z |
| institution | BVB |
| isbn | 3527333088 9783527333080 9783527664160 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-027523349 |
| oclc_num | 878979316 |
| open_access_boolean | |
| owner | DE-188 DE-11 DE-703 DE-19 DE-BY-UBM DE-29T |
| owner_facet | DE-188 DE-11 DE-703 DE-19 DE-BY-UBM DE-29T |
| physical | XVIII, 417 S. Ill., graph. Darst. |
| publishDate | 2015 |
| publishDateSearch | 2015 |
| publishDateSort | 2015 |
| publisher | Wiley-VCH |
| record_format | marc |
| spelling | Bioinspired catalysis metal-sulfur complexes ed. by Wolfgang Weigand ... Weinheim Wiley-VCH 2015 XVIII, 417 S. Ill., graph. Darst. txt rdacontent n rdamedia nc rdacarrier Katalyse (DE-588)4029921-1 gnd rswk-swf Grüne Chemie (DE-588)7563215-9 gnd rswk-swf Biokatalyse (DE-588)4393622-2 gnd rswk-swf Eisenverbindungen (DE-588)4151629-1 gnd rswk-swf Katalysator (DE-588)4029919-3 gnd rswk-swf Redoxreaktion (DE-588)4177303-2 gnd rswk-swf Schwefelverbindungen (DE-588)4180438-7 gnd rswk-swf (DE-588)4143413-4 Aufsatzsammlung gnd-content Redoxreaktion (DE-588)4177303-2 s Katalysator (DE-588)4029919-3 s Eisenverbindungen (DE-588)4151629-1 s Schwefelverbindungen (DE-588)4180438-7 s Grüne Chemie (DE-588)7563215-9 s DE-604 Katalyse (DE-588)4029921-1 s Biokatalyse (DE-588)4393622-2 s Weigand, Wolfgang 1958- (DE-588)1062586395 edt Erscheint auch als Online-Ausgabe, EPUB 978-3-527-66418-4 Erscheint auch als Online-Ausgabe, MOBI 978-3-527-66417-7 Erscheint auch als Online-Ausgabe, PDF 978-3-527-66419-1 X:MVB text/html http://deposit.dnb.de/cgi-bin/dokserv?id=4642567&prov=M&dok_var=1&dok_ext=htm Inhaltstext DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027523349&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Bioinspired catalysis metal-sulfur complexes Katalyse (DE-588)4029921-1 gnd Grüne Chemie (DE-588)7563215-9 gnd Biokatalyse (DE-588)4393622-2 gnd Eisenverbindungen (DE-588)4151629-1 gnd Katalysator (DE-588)4029919-3 gnd Redoxreaktion (DE-588)4177303-2 gnd Schwefelverbindungen (DE-588)4180438-7 gnd |
| subject_GND | (DE-588)4029921-1 (DE-588)7563215-9 (DE-588)4393622-2 (DE-588)4151629-1 (DE-588)4029919-3 (DE-588)4177303-2 (DE-588)4180438-7 (DE-588)4143413-4 |
| title | Bioinspired catalysis metal-sulfur complexes |
| title_auth | Bioinspired catalysis metal-sulfur complexes |
| title_exact_search | Bioinspired catalysis metal-sulfur complexes |
| title_full | Bioinspired catalysis metal-sulfur complexes ed. by Wolfgang Weigand ... |
| title_fullStr | Bioinspired catalysis metal-sulfur complexes ed. by Wolfgang Weigand ... |
| title_full_unstemmed | Bioinspired catalysis metal-sulfur complexes ed. by Wolfgang Weigand ... |
| title_short | Bioinspired catalysis |
| title_sort | bioinspired catalysis metal sulfur complexes |
| title_sub | metal-sulfur complexes |
| topic | Katalyse (DE-588)4029921-1 gnd Grüne Chemie (DE-588)7563215-9 gnd Biokatalyse (DE-588)4393622-2 gnd Eisenverbindungen (DE-588)4151629-1 gnd Katalysator (DE-588)4029919-3 gnd Redoxreaktion (DE-588)4177303-2 gnd Schwefelverbindungen (DE-588)4180438-7 gnd |
| topic_facet | Katalyse Grüne Chemie Biokatalyse Eisenverbindungen Katalysator Redoxreaktion Schwefelverbindungen Aufsatzsammlung |
| url | http://deposit.dnb.de/cgi-bin/dokserv?id=4642567&prov=M&dok_var=1&dok_ext=htm http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=027523349&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT weigandwolfgang bioinspiredcatalysismetalsulfurcomplexes |