Handbook of flavoproteins: 2 Complex flavoproteins, dehydrogenases and physical methods
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| Format: | Buch |
| Sprache: | German |
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Berlin [u.a.]
De Gruyter
2013
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| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XV,436 S. Ill.,graph. Darst. |
| ISBN: | 9783110298284 |
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| 245 | 1 | 0 | |a Handbook of flavoproteins |n 2 |p Complex flavoproteins, dehydrogenases and physical methods |c ed. by Russ Hille ... |
| 264 | 1 | |a Berlin [u.a.] |b De Gruyter |c 2013 | |
| 300 | |a XV,436 S. |b Ill.,graph. Darst. | ||
| 336 | |b txt |2 rdacontent | ||
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IMAGE 1
TABLE OF CONTENTS
PREFACE V
1 THE REACTION MECHANISMS OF CROUPS A AND B FLAVOPROTEIN MONOOXYGENASES
1
1.1 INTRODUCTION 1
1.2 ENZYMES ACTING UPON AROMATIC SUBSTRATES - C R O U P A 2
1.2.1 REACTIONS CATALYZED 2
1.2.2 PROTEIN STRUCTURES 3
1.2.3 DETAILED MECHANISM O F PHBH 4
1.2.3.1 REDUCTIVE HALF-REACTION 6
1.2.3.2 OXIDATIVE HALF-REACTION 9
1.2.3.3 HYDROXYLATION CHEMISTRY 15
1.2.3.4 SUMMARY 16
1.3 ENZYMES ACTING UPON NON-AROMATIC SUBSTRATES - GROUP B 16
1.3.1 REACTIONS CATALYZED AND SUBCLASSES 16
1.3.1.1 B V M O S 17
1.3.1.2 FMOS 19
1.3.1.3 N M O S 2 0
1.3.1.4 YUCCAS 21
1.3.2 STRUCTURAL FEATURES 22
1.4 REFERENCES 23
2 FLAVIN-DEPENDENT MONOOXYGENASES IN SIDEROPHORE BIOSYNTHESIS 2 9
2.1 IRON, AN ESSENTIAL BUT SCARCE NUTRIENT 2 9
2.2 SIDEROPHORES 3 0
2.2.1 SIDEROPHORES ARE IMPORTANT VIRULENCE FACTORS 3 0
2.2.2 STRUCTURAL DIVERSITY O F SIDEROPHORES 33
2.3 FLAVIN-DEPENDENT N-HYDROXYLATING MONOOXYGENASES 33
2.4 CATALYTIC CYCLE O F N M O S 3 4
2.4.1 FLAVIN REDUCTION IN N M O S 35
2.4.2 FLAVIN OXIDATION IN N M O S 3 7
2.5 THREE-DIMENSIONAL STRUCTURE O F N M O S 3 7
2.5.1 FAD-BINDING DOMAIN 4 0
2.5.2 N A D P H - B I N D I N G D O M A I N 4 0
2.5.3 L - O R N I T H I N E - B I N D I N G DOMAIN 41
2.6 THE STRUCTURAL BASIS O F SUBSTRATE SPECIFICITY IN N M O S 42
2.7 MECHANISM O F STABILIZATION O F THE C4A-HYDROPEROXYFLAVIN B Y N A D
P + . . . 42 2.8 ACTIVATION O F N M O S B Y A M I N O ACID BINDING 4 4
2.9 UNUSUAL N M O S 4 4
2.10 FLIGH-THROUGHPUT SCREENING ASSAY TO IDENTIFY INHIBITORS O F N M O S
45
2.11 CONCLUSIONS 4 6
2.12 REFERENCES 4 7
HTTP://D-NB.INFO/1023223295
IMAGE 2
X TABLE OF CONTENTS
3 THE FLAVIN MONOOXYGENASES 51
3.1 INTRODUCTION 51
3.2 OCCURRENCE AND CLASSIFICATION 5 4
3.2.1 A M I N O ACID SEQUENCE MOTIFS 5 4
3.2.2 D N A SCREENING 55
3.3 SINGLE-COMPONENT FLAVIN MONOOXYGENASES 5 6
3.3.1 SUBCLASS A 5 6
3.3.2 SUBCLASS B 5 8
3.3.3 SUBCLASS C 6 0
3.3.4 SUBCLASS D 61
3.3.5 SUBCLASS E 62
3.3.6 SUBCLASS F 62
3.4 CONCLUSIONS 6 4
3.5 REFERENCES 65
4 STRUCTURE AND CATALYTIC MECHANISM OF NADPH-CYTOCHROME P450
OXIDOREDUCTASE: A PROTOTYPE OF THE DIFLAVIN OXIDOREDUCTASE FAMILY OF
ENZYMES 73
4.1 INTRODUCTION 73
4.2 PROPERTIES O F CYPOR FLAVINS 75
4.3 DOMAIN STRUCTURE AND FUNCTION 78
4.4 MEMBRANE BINDING DOMAIN (MBD) 78
4.5 FMN DOMAIN 79
4.6 CYTOCHROME P450 BINDING: ROLE O F THE F M N DOMAIN AND CONNECTING
DOMAIN 8 0
4.7 FAD DOMAIN 82
4.8 MECHANISM O F HYDRIDE TRANSFER 82
4.9 INTERFLAVIN ELECTRON TRANSFER 83
4.10 FMN TO HEME ELECTRON TRANSFER 85
4.11 P450 CATALYSIS 85
4.12 OTHER CYPOR ELECTRON ACCEPTORS 87
4.13 CYPOR DOMAIN MOVEMENT AND CONTROL O F ELECTRON TRANSFER 8 7
4.14 PHYSIOLOGICAL FUNCTIONS O F CYPOR AND EFFECTS O F CYPOR DEFICIENCY
. 9 0 4.15 H U M A N CYPOR DEFICIENCY (PORD) 91
4.16 CONTRIBUTION O F CYPOR TO INTER-INDIVIDUAL VARIATION IN H U M A N
DRUG METABOLISM 92
4.1 7 UNANSWERED QUESTIONS AND FUTURE DIRECTIONS 92
4.18 REFERENCES 93
5 THE XANTHINE OXIDOREDUCTASE ENZYME FAMILY: XANTHINE DEHYDROGENASE,
XANTHINE OXIDASE, AND ALDEHYDE OXIDASE 1 03
5.1 INTRODUCTION 103
5.2 OVERALL STRUCTURES 104
5.3 REACTION MECHANISM 105
5.4 ELECTRON TRANSFER FROM THE MOLYBDENUM CENTER TO OTHER REDOX-ACTIVE
CENTERS 113
5.5 REACTION O F FAD W I T H N A D + O R MOLECULAR OXYGEN 114
IMAGE 3
TABLE OF CONTENTS | X I
5.6 INHIBITORS O F XANTHINE OXIDOREDUCTASE 116
5.7 REFERENCES 120
6 ASSIMILATORY NITRATE REDUCTASE 125
6.1 INTRODUCTION AND SCOPE 125
6.2 ENZYME STRUCTURE 126
6.3 KINETICS AND MECHANISM 131
6.4 POST-TRANSLATIONAL REGULATION 133
6.5 INTERCONVERSION O F SULFITE OXIDASE AND NITRATE REDUCTASE ACTIVITIES
135
6.6 CONCLUSIONS 137
6.7 REFERENCES 138
7 SUCCINATE DEHYDROGENASE (COMPLEX II) AND FUMARATE REDUCTASE 141
7.1 HISTORY O F COMPLEX II 141
7.2 O V E R V I E W O F C O M P L E X II 143
7.3 STRUCTURE O F COMPLEX II 144
7.4 CATALYTIC ASSAYS 146
7.5 CATALYTIC MECHANISM AND DOMAIN MOVEMENT 148
7.6 ELECTRON TRANSFER 151
7.7 Q U I N O N E - B I N D I N G SITE O F COMPLEX II 153
7.8 ASSEMBLY O F THE COVALENT FAD COFACTOR INTO COMPLEX II 155
7.9 CONCLUDING REMARKS 159
7.10 REFERENCES 159
8 FLAVOPROTEIN DISULFIDE REDUCTASES AND STRUCTURALLY RELATED
FLAVOPROTEIN THIOL/DISUIFIDE-LINKED OXIDOREDUCTASES 165
8.1 INTRODUCTION 165
8.2 GROUP 1 FDR ENZYMES: CLASSIC DITHIOL/DISULFIDE OXIDOREDUCTASES W I T
H A SINGLE CXXXXC DISULFIDE REDOX CENTER 169
8.2.1 DIHYDROLIPOAMIDE DEHYDROGENASE (LIPDH) 174
8.2.2 GLUTATHIONE REDUCTASE (GR) - T W O N E W STRUCTURAL STUDIES ON
THIS CLASSIC MEMBER O F THE GROUP 176
8.2.3 TRYPANOTHIONE REDUCTASE (TRYR) 177
8.2.4 M Y C O T H I O N E REDUCTASE (MYCR) 177
8.3 G R O U P 2 A FDR ENZYMES - ENZYMES O F THE GROUP 1 STRUCTURAL FOLD
REQUIRING AN ADDITIONAL C-TERMINAL CYS-BASED REDOX CENTER 177
8.3.1 MERCURIC ION REDUCTASE (MERA) 180
8.3.2 HIGH /V) R T H I O R E D O X I N REDUCTASES (TRXR AND TGR) 181
8.4 G R O U P 2B FDR ENZYMES - L O W M THIOREDOXIN REDUCTASE (TRXR) AND
STRUCTURALLY RELATED ENZYMES 183
8.5 GROUP 3 FDR ENZYMES - ENZYMES W I T H CYSTEINE SULFENIC ACID OR
MIXED CYS-S-S-COA REDOX CENTER 188
8.6 G R O U P 4 FDR ENZYMES - GROUP 1 -FOLD ENZYMES CATALYZING NOVEL
REACTIONS 192
8.7 G R O U P 5 FDR ENZYMES - ENZYMES W I T H A SI SIDE PAIR O F CYS
RESIDUES W I D E L Y SEPARATED IN SEQUENCE 194
8.8 REFERENCES 196
IMAGE 4
XII | TABLE OF CONTENTS
9 FLAVOENZYMES IN PYRIMIDINE METABOLISM 203
9.1 INTRODUCTION 203
9.2 PYRIMIDINE/DIHYDROPYRIMIDINE INTERCONVERSIONS 2 0 4
9.2.1 O V E R V I E W 2 0 4
9.2.2 DIHYDROOROTATE DEHYDROGENASES 2 0 6
9.2.2.1 GENERAL 2 0 6
9.2.2.2 MECHANISMS O F THE PYRIMIDINE HALF-REACTIONS 2 0 7
9.2.2.3 MECHANISMS OF THE NON-PYRIMIDINE HALF-REACTIONS 2 1 0
9.2.3 DIHYDROURIDINE SYNTHASES 213
9.2.3.1 GENERAL 213
9.2.3.2 PYRIMIDINE HALF-REACTIONS 2 1 4
9.2.3.3 NON-PYRIMIDINE HALF-REACTION 2 1 4
9.2.4 D I H Y D R O P Y R I M I D I N E DEHYDROGENASES 2 1 4
9.2.4.1 GENERAL 2 1 4
9.2.4.2 PYRIMIDINE HALF-REACTION 2 1 5
9.3 METHYLATIONS 2 1 5
9.3.1 O V E R V I E W 2 1 5
9.3.2 FLAVIN-DEPENDENT THYMIDYLATE SYNTHASE 2 1 6
9.3.3 FOLATE/FAD-DEPENDENT METHYL TRANSFERASE (TRMFO) 2 1 8
9.4 REFERENCES 2 2 1
10 EXCITED STATE ELECTRONIC STRUCTURE OF FLAVINS AND FLAVOPROTEINS FROM
THEORY AND EXPERIMENT 2 2 5
10.1 INTRODUCTION 225
10.2 FLAVIN PHOTOPHYSICS AND THE ELECTRONIC STRUCTURE O F ITS EXCITED
STATES 2 2 7
10.2.1 MOMENTS O F THE CHARGE DISTRIBUTION 2 2 7
10.2.2 EXPERIMENTAL TECHNIQUES FOR THE DETERMINATION O F EXCITED STATE
ELECTRONIC STRUCTURE 2 2 8
10.3 LINEAR DICHROISM MEASUREMENTS O F REDUCED ANIONIC FLAVIN TRANSITION
DIPOLE MOMENTS AND COMPLIMENTARY CALCULATIONS 2 2 9
10.4 EXPERIMENTAL STUDIES O F EXCITED STATE ELECTRONIC STRUCTURE O F
FLAVINS AND COMPLEMENTARY CALCULATIONS 2 3 0
10.4.1 O X I D I Z E D FLAVIN 2 3 0
10.4.2 EXCITED STATE STRUCTURE O F OYE AND OYE CHARGE TRANSFER COMPLEX
232
10.4.3 D N A PHOTOLYASE AND 2 3 4
10.4.4 EXPERIMENTAL RESULTS FOR THE FLAVIN NEUTRAL RADICAL 2 3 6
10.5 COMPUTATIONAL STUDIES ON FLAVINS 2 3 8
10.5.1 CALCULATIONS FOR OXIDIZED FLAVINS 2 3 8
10.5.2 COMPUTATIONAL RESULTS FOR SEMIQUINONE FLAVIN 2 4 0
10.5.3 COMPUTATIONAL STUDIES O N REDUCED FLAVINS 2 4 1
10.6 SPECTROSCOPIC STUDIES BEARING ON EXCITED ELECTRONIC STATES O F
FLAVINS 243 10.6.1 TIME-RESOLVED STUDIES O F OXIDIZED FLAVIN 243
10.6.2 THE TRIPLET STATE O F FLAVINS 2 4 4
10.7 PHOTOINDUCED ELECTRON TRANSFER IN FLAVINS 2 4 4
10.8 APPLICATIONS O F FLAVIN PHOTOCHEMISTRY 245
IMAGE 5
TABLE OF CONTENTS | XIII
10.9 CONCLUSIONS 2 4 6
10.10 REFERENCES 2 4 6
11 STRUCTURAL PROPERTIES OF THE ALKANESULFONATE MONOOXYGENASE SYSTEM
THAT DICTATE FUNCTION 255
11.1 INTRODUCTION 2 5 5
11.2 SULFUR LIMITATION IN BACTERIAL SYSTEMS 2 5 6
11.3 F M N REDUCTASE O F THE ALKANESULFONATE MONOOXYGENASE SYSTEM 2 5 8
11.4 MONOOXYGENASE ENZYMES O F THE BACTERIAL LUCIFERASE FAMILY 2 5 9
11.4.1 STRUCTURAL PROPERTIES O F THE BACTERIAL LUCIFERASE FAMILY 2 5 9
11.4.2 STRUCTURAL DYNAMICS O F ALKANESULFONATE MONOOXYGENASE 261 11.4.3
ACTIVE SITE STRUCTURE IN THE BACTERIAL LUCIFERASE FAMILY 263
11.4.4 CATALYTIC MECHANISMS O F THE BACTERIAL LUCIFERASE FAMILY 265
11.4.5 MECHANISTIC PROPERTIES O F ALKANESULFONATE MONOOXYGENASE. 265
11.5 MECHANISM O F FLAVIN TRANSFER 2 6 9
11.6 CONCLUSIONS 271
11.7 REFERENCES 271
12 SINGLE MOLECULE METHODS TO STUDY FLAVOPROTEINS 2 7 7
12.1 FLAVOPROTEINS AND ELECTRON-TRANSFER REACTIONS 2 7 7
12.2 BULK VS. SINGLE-MOLECULE METHODS 2 7 8
12.3 SINGLE-MOLECULE TECHNIQUES FOR THE STUDY O F BIOLOGICAL SYSTEMS 2 7
9
12.3.1 A T O M I C FORCE MICROSCOPY 2 8 0
12.3.2 OPTICAL TWEEZERS 282
12.3.3 A F M BASED FORCE SPECTROSCOPY 2 8 4
12.3.3.1 THE AVIDIN-BIOTIN C O M P L E X 2 8 6
12.3.3.2 ANTIGEN-ANTIBODY INTERACTION 2 8 7
12.3.3.3 MOLECULAR INTERACTIONS IN TRANSIENT COMPLEXES 2 8 7
12.4 SINGLE-MOLECULE EXPERIMENTS W I T H FLAVOENZYMES 2 8 8
12.4.1 FLUORESCENCE MEASUREMENTS 2 8 8
12.4.2 FORCE MEASUREMENTS IN FLAVOPROTEINS 2 9 0
12.5 REFERENCES 295
13 APPLICATIONS O F SACCHAROMYCES PASTORIANUS OLD YELLOW ENZYME TO
ASYMMETRIC ALKENE REDUCTIONS 2 9 9
13.1 IDENTIFICATION AND INITIAL CHARACTERIZATION 2 9 9
13.1.1 HISTORY O F OYE1 2 9 9
13.1.2 OYE 1 STRUCTURE AND ROLES O F KEY RESIDUES 301
13.1.2.1 HISTIDINE 191 AND ASPARAGINE 194 302
13.1.2.2 TYROSINE 196 302
13.1.2.3 THREONINE 3 7 302
13.1.2.4 TRYPTOPHAN 116 3 0 4
13.2 SUBSTRATE SPECIFICITY O F OYE 1 305
13.2.1 KETONES AND ALDEHYDES 3 0 6
13.2.2 ESTERS 312
13.2.3 NITRO ALKENES 315
13.3 CONCLUSIONS 3 1 7
13.4 REFERENCES 3 1 8
IMAGE 6
XIV TABLE OF CONTENTS
14 CONTRIBUTIONS OF PROTEIN ENVIRONMENT TO THE REDUCTION POTENTIALS
OF FLAVIN-CONTAINING PROTEINS 321
14.1 INTRODUCTION 321
14.2 COMPUTATION O F Q/HQ O N THE BASIS O F THE CRYSTAL STRUCTURES 322
14.3 CALCULATION O F SQ/HQ AND DETERMINATION O F REDOX-LINKED A M I N
O ACID RESIDUES 3 2 4
14.4 INFLUENCE O F THE PROTEIN BACKBONE CONFORMATION ON 325
14.5 INFLUENCE O F THE LOOP REGION NEAR THE FLAVIN BINDING SITE ON 3 2
6
14.6 INFLUENCE O F THE F M N PHOSPHATE GROUP ON SC|/HQ 3 2 9
14.7 CONCLUSIONS 332
14.8 REFERENCES 332
15 METHODS BASED ON CONTINUUM ELECTROSTATICS AND THEIR APPLICATION TO
FLAVOPROTEINS - A REVIEW 3 3 5
15.1 INTRODUCTION 335
15.2 THE CONTINUUM ELECTROSTATIC MODEL BASED ON THE POISSON-BOLTZMANN
EQUATION 3 3 6
15.2.1 THE PHYSICAL BASIS O F THE POISSON-BOLTZMANN EQUATION 3 3 6
15.2.2 ELECTROSTATIC POTENTIALS AND ELECTROSTATIC ENERGIES 3 3 9
15.3 ASSOCIATION O F FLAVOPROTEINS 341
15.3.1 ELECTROSTATIC DOCKING O F FLAVOPROTEINS 341
15.3.2 SIMILARITY O F ELECTROSTATIC POTENTIALS O F PROTEINS 342
15.4 TITRATION BEHAVIOR O F PROTEINS 3 4 4
15.4.1 MICROSTATE MODEL 345
15.4.2 DTPA - A N ILLUSTRATIVE EXAMPLE 3 4 6
15.4.3 THEORETICAL ANALYSIS O F THE PROTONATION O F FLAVOPROTEINS 3 4 9
15.5 RECENT AND UPCOMING DEVELOPMENTS 352
15.6 REFERENCES 3 5 4
16 FLAVOPROTEINS AND BLUE LIGHT RECEPTION IN PLANTS 361
16.1 INTRODUCTION (LIGHT RECEPTION IN PLANTS) 361
16.2 PLANT PHOTOTROPINS 363
16.2.1 L O V DOMAIN STRUCTURE 3 6 4
16.2.2 L O V PHOTOCHEMISTRY 365
16.2.3 L O V SIGNAL PROPAGATION 3 6 9
16.3 CRYPTOCHROMES 371
16.3.1 CRYPTOCHROME STRUCTURE 371
16.3.2 CRYPTOCHROME PHOTOCHEMISTRY 3 7 4
16.3.3 CRYPTOCHROME SIGNAL TRANSDUCTION 3 7 8
16.4 O U T L O O K 3 8 0
16.5 REFERENCES 381
17 ULTRAFAST DYNAMICS OF FLAVINS AND FLAVOPROTEINS 393
17.1 INTRODUCTION 393
17.2 ULTRAFAST DYNAMICS O F FLAVINS 3 9 4
17.2.1 STEADY-STATE SPECTROSCOPIC PROPERTIES 3 9 4
17.2.2 O X I D I Z E D FLAVINS 3 9 6
IMAGE 7
TABLE OF CONTENTS | XV
17.2.3 A N I O N I C AND NEUTRAL RADICAL FLAVINS 3 9 8
17.2.4 A N I O N I C AND NEUTRAL FULLY-REDUCED FLAVINS 3 9 9
17.3 ELECTRON TRANSFER IN MODEL FLAVODOXIN 401
17.3.1 EXPERIMENT DESIGN, REACTION SCHEME AND PROBING STRATEGY 401
17.3.2 FEMTOSECOND CHARGE SEPARATION, FROZEN ACTIVE-SITE CONFIGURATION
AND CRITICAL FREE ENERGIES 403
1 7.3.3 ULTRAFAST CHARGE RECOMBINATION, VIBRATIONAL QUANTUM EFFECT AND
HOT GROUND-STATE COOLING 4 0 4
1 7.3.4 PHOTOINDUCED REDOX CYCLE, REACTION TIME SCALES, AND VIBRATIONAL
COUPLING GENERALITY 4 0 6
1 7.4 ENZYMATIC REACTIONS AND REPAIR PHOTOCYCLES IN D N A PHOTOLYASES 4
0 8
1 7.4.1 DYNAMICS AND MECHANISM O F CYCLOBUTANE PYRIMIDINE DIMER REPAIR B
Y CPD PHOTOLYASE 4 0 8
1 7.4.1.1 SEQUENTIAL SPLITTING DYNAMICS O F THE CYCLOBUTANE RING 4 0 8
17.4.1.2 ELECTRON TUNNELING PATHWAYS AND FUNCTIONAL ROLE O F ADENINE
MOIETY 4 1 0
1 7.4.2 DYNAMICS AND MECHANISM O F REPAIR O F UV-INDUCED (6-4)
PHOTOPRODUCT B Y (6-4) PHOTOLYASE 4 1 4
1 7.4.2.1 ULTRAFAST ELECTRON AND PROTON TRANSFER DYNAMICS 4 1 6
17.4.2.2 CATALYTIC REPAIR PHOTOCYCLE 4 1 7
17.5 SIGNAL TRANSDUCTION IN BLUE-LIGHT PHOTORECEPTORS 4 1 9
1 7.5.1 PHOTOADDITION O F CYSTEINE TO FLAVIN IN PHOTOTROPIN 4 1 9
17.5.2 SWITCHING O F FLAVIN HYDROGEN BOND IN BLUF PROTEIN 4 1 9
1 7.5.3 ULTRAFAST FLAVIN DYNAMICS IN CRYPTOCHROME 4 2 0
17.6 CONCLUSIONS 4 2 0
17.7 REFERENCES 421
INDEX 4 2 9 |
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| physical | XV,436 S. Ill.,graph. Darst. |
| publishDate | 2013 |
| publishDateSearch | 2013 |
| publishDateSort | 2013 |
| publisher | De Gruyter |
| record_format | marc |
| spelling | Handbook of flavoproteins 2 Complex flavoproteins, dehydrogenases and physical methods ed. by Russ Hille ... Berlin [u.a.] De Gruyter 2013 XV,436 S. Ill.,graph. Darst. txt rdacontent n rdamedia nc rdacarrier (DE-588)4143413-4 Aufsatzsammlung gnd-content Hille, Russ (DE-588)1029934789 edt (DE-604)BV041000514 2 DNB Datenaustausch application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=026197525&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Handbook of flavoproteins |
| subject_GND | (DE-588)4143413-4 |
| title | Handbook of flavoproteins |
| title_auth | Handbook of flavoproteins |
| title_exact_search | Handbook of flavoproteins |
| title_full | Handbook of flavoproteins 2 Complex flavoproteins, dehydrogenases and physical methods ed. by Russ Hille ... |
| title_fullStr | Handbook of flavoproteins 2 Complex flavoproteins, dehydrogenases and physical methods ed. by Russ Hille ... |
| title_full_unstemmed | Handbook of flavoproteins 2 Complex flavoproteins, dehydrogenases and physical methods ed. by Russ Hille ... |
| title_short | Handbook of flavoproteins |
| title_sort | handbook of flavoproteins complex flavoproteins dehydrogenases and physical methods |
| topic_facet | Aufsatzsammlung |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=026197525&sequence=000001&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| volume_link | (DE-604)BV041000514 |
| work_keys_str_mv | AT hilleruss handbookofflavoproteins2 |