Iron-containing enzymes: versatile catalysts of hydroxylation reactions in nature
Gespeichert in:
| Format: | Buch |
|---|---|
| Sprache: | English |
| Veröffentlicht: |
Cambridge
RSC Publ.
2011
|
| Schlagworte: | |
| Online-Zugang: | Inhaltsverzeichnis |
| Beschreibung: | XIII, 448 S. : Ill., graph. Darst. 24 cm |
| ISBN: | 9781849731812 1849731810 |
Internformat
MARC
| LEADER | 00000nam a2200000 c 4500 | ||
|---|---|---|---|
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| 003 | DE-604 | ||
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| 008 | 120821s2011 ad|| |||| 00||| eng d | ||
| 020 | |a 9781849731812 |c (hbk.) £139.99 |9 978-1-84973-181-2 | ||
| 020 | |a 1849731810 |c (hbk.) £139.99 |9 1-84973-181-0 | ||
| 035 | |a (OCoLC)812242426 | ||
| 035 | |a (DE-599)BSZ348346794 | ||
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| 084 | |a CHE 376f |2 stub | ||
| 245 | 1 | 0 | |a Iron-containing enzymes |b versatile catalysts of hydroxylation reactions in nature |c ed. by Sam P. de Visser ... |
| 246 | 1 | 0 | |a iron-containing |
| 264 | 1 | |a Cambridge |b RSC Publ. |c 2011 | |
| 300 | |a XIII, 448 S. : |b Ill., graph. Darst. |c 24 cm | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
| 338 | |b nc |2 rdacarrier | ||
| 650 | 0 | 7 | |a Katalyse |0 (DE-588)4029921-1 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Eisenkomplexe |0 (DE-588)4222910-8 |2 gnd |9 rswk-swf |
| 650 | 0 | 7 | |a Enzym |0 (DE-588)4014988-2 |2 gnd |9 rswk-swf |
| 653 | |a Metalloenzymes | ||
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| 689 | 0 | |5 DE-604 | |
| 700 | 1 | |a Visser, Sam P. de |e Sonstige |4 oth | |
| 856 | 4 | 2 | |m Digitalisierung UB Regensburg - ADAM Catalogue Enrichment |q application/pdf |u http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025227918&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |3 Inhaltsverzeichnis |
| 999 | |a oai:aleph.bib-bvb.de:BVB01-025227918 | ||
Datensatz im Suchindex
| _version_ | 1804149422704033792 |
|---|---|
| adam_text | Contents
Chapter
1
Experimental and Computational Studies on the Catalytic
Mechanism of Non-heme Iron Dioxygenases
1
Sam P.
de Visser
1.1
Introduction
1
1.2
a-Ketoglutarate Dependent Dioxygenases (aKDD)
and
Halogenases (ocKDH)
3
1.2.1
Taurine/
a-Ketoglutarate Dioxygenase (TauD)
4
1.2.2
AlkB Repair Enzymes
10
1.2.3
Prolyl-4-hydroxylase
(P4H)
10
1.2.4
a-Ketoglutarate Dependent
Halogenases
(aKDH)
17
1.3
Cysteine
Dioxygenase (CDO)
21
1.4
Isopenicillin
TV Synthase (IPNS)
27
1.5 1 -
Aminocyclopropane-
1
-carboxy lie
Acid
Oxidase (ACCO)
30
1.6
Rieske Dioxygenases
32
1.7
Extradiol and Intradiol Dioxygenases
34
1.8
Conclusion
35
References
36
Chapter
2
Non-heme Iron-Dependent Dioxygenases: Mechanism
and Structure
42
Timothy D. H.
Bugg
2.1
Introduction
42
2.2
Dioxygenases Catalysing Oxidative C-C
Cleavage Reactions
43
VII
viii Contents
2.2.1
Intradiol Catechol Dioxygenases
43
2.2.2
Extradiol Catechol Dioxygenases
46
2.2.3
Carotenoid
Cleavage
Dioxygenases
49
2.2.4
Oxidative
Cleavage of Aliphatic Substrates
50
2.3
Dioxygenases
Catalysing Formation
of Peroxides: Lipoxygenases
55
2.4
Dioxygenases Catalysing Hydroxylation Reactions
57
2.4.1
α
-Ketoghitarate-Dependent
Dioxygenases
57
2.4.2
Arene
(Rieske) Dioxygenases
59
2.5
Conclusion and Summary
62
References
63
Chapter
3
Transient Iron Species in the Catalytic Mechanism of the
Archetypal oc-Ketoglutarate-Dependent Dioxygenase, TauD
67
Denis A. Proshlyakov and Robert P.
Hausinger
3.1
Introduction
67
3.2
Structure of the TauD Active Site
68
3.2.1
Metal Binding to TauD Apoprotein
69
3.2.2
Substrate Binding to TauD
70
3.2.3
Characterization of the NO-Bound
Quaternary Complex
71
3.3
The Fe(iv)-oxo Species
72
3.3.1
Experimental Detection of Fe(iv)-oxo
72
3.3.2
Electronic Configuration of the
Fe(iv)-oxo Species
74
3.3.3
Hydrogen Atom Abstraction by Fe(iv)-oxo
76
3.3.4
Thermodynamics of Hydrogen Atom
Abstraction by Fe(iv)-oxo
77
3.4
Fe(in)-O(H) Species and Oxygen Transfer
80
3.5
Conclusions
83
Acknowledgements
84
References
84
Chapter
4
Density Functional Theory Studies on Non-heme
Iron Enzymes
88
Tomasz
Bor
o w
ski and Per
Ε. Μ.
Siegbahn
4.1
Introduction
88
4.1.1
Reactions Catalysed by Non-heme Iron
Enzymes and their Biological Significance
89
4.1.2
Iron Binding Sites
91
4.2
Computational Methods
93
4.3
Dioxygen Binding and Generation of Peroxo
Intermediates
94
Contents ix
4.3.1 O2
Binding with Oxidation of
Fe(ii)
94
4.3.2
O2 Binding with Oxidation of the
Organic Substrate
96
4.3.3
O2 Binding with Oxidation of External
Reductants
98
4.4
Strategies for
О
-O
Bond Cleavage
98
4.4.1
Heterolytic
О
-O
Bond Cleavage Leading
to Fe(iv)=O
99
4.4.2
Homolytic
О
-O
Bond Cleavage Leading
to R-O*
101
4.4.3
Heterolytic
О
-O
Bond Cleavage in
FeOnbOOH
103
4.5
Reactions of the High-
Valent
Intermediates
104
4.5.1
Oxygénation
by Fe(iv)=O
104
4.5.2
Oxidation by Fe(iv)=O
107
4.5.3
Reactions of R-O
* 110
4.6
Origins of Chemoselectivity
—
The Role of Negative
Catalysis
112
4.7
Conclusions
114
References 1
14
Chapter
5
Theoretical Spectroscopies of Iron-Containing Enzymes
and Biomimetics
119
Shengfa Ye, Gemma
J
.
Christian, Caiyim Geng and
Frank Neese
5.1
Introduction
119
5.2
Mössbauer
Spectroscopy
120
5.2.1
Theoretical Prediction of
Mössbauer
Parameters
121
5.2.2
Examples from the Literature
123
5.3
Nuclear Resonance Vibrational Spectroscopy
125
5.3.1
Examples from the Literature
126
5.4
Electron Paramagnetic Resonance
127
5.4.1
Theoretical EPR Spectroscopy
127
5.4.2
Examples from the Literature
130
5.5
Absorption Spectroscopy
133
5.5.1
Theoretical Prediction of Absorption
Spectroscopy
133
5.5.2
Examples from the Literature
134
5.6
Х
-Ray Spectroscopy
136
5.6.1
Theoretical Prediction of Metal and Ligand
 -Edge
Spectra
137
5.6.2
Examples from the Literature
138
5.7
Conclusion
139
References
140
χ
Contents
Chapter
6
Bioinspired
Non-heme
Iron Catalysts in
C
-Н
and C=C
Oxidation Reactions
148
Anna Company, Laura Gomez and
Miquel Costas
6.1
Biological Precedents
148
6.1.1
Oxidad ve
Iron Proteins
149
6.1.2
Cytochrome P450
150
6.1.3
Rieske Dioxygenases
151
6.2
Non-heme Iron Complexes as
Bioinspired Catalysts
154
6.2.1
Oxidation of Alkanes
(C
-Н
Bonds) by
Non-heme Iron Complexes
155
6.2.2
Oxidation of Alkenes (C=C Double Bonds)
by Non-heme Iron Complexes
175
6.3
Reaction Mechanisms in Catalytic C~H
and C=C Oxidation Reactions Mediated by
Complexes with N-Rich Ligands
187
6.3.1
The Initially Formed Fe -OOH and its
Cleavage Products
187
6.3.2
Olefin
Oxidations: Epoxidation and
¿■/.ç-Dihydroxylation
189
6.3.3
Alkane Oxidations
198
6.4
Conclusions
201
References
202
Chapter
7
Application of Magnetic Circular Dichroism, X-Ray
Absorption Spectroscopy and Extended
Х
-Ray Absorption
Fine Structure in Determining Geometric and Electronic
Structure of Non-heme Iron(iv)-oxo Enzymatic Intermediates
and Related Synthetic Models
209
Somdatta Ghosh
Dey
and Abhishek
Dey
7.1
Introduction
209
7.1.1
Magnetic Circular Dichroism (MCD)
212
7.1.2
Х
-Ray Absorption Spectroscopy and
Extended
Х
-Ray Absorption Fine Structure
223
7.2
MCD of Iron(iv)-oxo Complexes
226
7.2.1
[Felv=O(TMC)(NCCH3)]2+
226
7.2.2
Iron(iv)-oxo MCD: Varying Axial and
Equatorial Ligands
230
7.2.3
Vibronic Progression in MCD
233
7.3
XAS
and EXAFS of Iron(iv)-oxo Intermediates
and Synthetic Model Complexes
236
7.3.1
Enzymatic Catalytic Cycle Intermediates
236
7.3.2
Model Complexes
245
Contents xi
7.4
Parting Thoughts
250
References
251
Chapter
8
Structure, Mechanism and Function of Cytochrome
P450 Enzymes
255
Kirs
t y J.
McLean, Hazel
M. G
ir
v
an, Amy
E.
Mason,
Adrian J. Dunford and Andrew W. Munro
8.1
Introduction
255
8.2
Cytochromes P450
-
A Brief History
256
8.3
Optical and
Spectroscopie
Features
257
8.4
Cytochrome P450 Catalytic Cycle
260
8.5
Biological Diversity
263
8.6
Cytochrome P450
Redox
Partner Systems
264
8.7
Cytochrome P450 Structure
267
8.8
Physiological Roles of Cytochromes P450
269
8.9
Cytochrome P450 Medicine and Biotechnology
272
8.10
Conclusions and Future Prospects
275
References
275
Chapter
9
Drug Metabolism by Cytochrome P450: A Tale of
Mult ¡state Reactivity
281
Dexesh Kumar
9.1
Introduction
281
9.2
Nomenclature of Cytochrome P450 Enzymes
282
9.3
Types of Drug Interactions
283
9.3.1
Induction
283
9.3.2
Inhibition
285
9.4
Important Isoforms of Human CYP
285
9.4.1
CYP1A2
Isoform 285
9.4.2
CYP2C8. CYP2C9 and CYP2C19 Isoforms
287
9.4.3
CYP2D6
Isoform 287
9.4.4
CYP3A4
Isoform 287
9.5
Examples of Generation of Various Metabolites
from a Single CYP
450 288
9.6
CYP
450
Structure
290
9.7
Catalytic Cycle of CYP
450 291
9.8
Compound I of CYP
450:
The Active Species
292
9.8.1
Axial Ligand Effect of Compound I
295
9.9
Reactiv
it> of Compound I
301
9.10
Aliphatic
C
-Н
Hydroxylation by Compound I
of CYP
450 303
9.10.1
Rearrangement Mechanisms of Aliphatic
Hydroxylation Reactions
308
9.11
C=Q Epoxidation by Compound I of CYP
450 312
xii
Contents
9.12
Sulfoxidation Reaction by Compound I of CYP
450 315
9.13
Aromatic Hydroxylation Reaction by Compound I
of CYP
450 317
9.14
Role of Water Molecule as Biocatalyst
319
9.15
Conclusion
321
Acknowledgements
321
References
321
Chapter
10
Oxidation of Unnatural Substrates by Engineered
Cytochrome P450CJun
330
Saptaswa Sen, Soumen
Kanti
Manna and
Shyamalava Mazumdar
10.1
Introduction
330
10.2
Binding of the Substrate
331
10.3
CYP 450cam Reaction Cycle
334
10.4
Rational Design of the Active Site of CYP 450cam
336
10.5
Metabolism of Unnatural Substrates by
CYP 450cam Variants
338
10.6
Binding of Unnatural Substrate, Hydroxylation,
and Product Release
339
10.6.1
Small Hydrocarbons
340
10.6.2
Alkyl
Benzenes
344
10.6.3
Polycyclic Aromatic Hydrocarbons (PAHs)
344
10.6.4
2-Ethylhexanol
345
10.6.5
Aromatic—Aliphatic Hydrocarbon,
Phenylcyclohexane
346
10.6.6
Diphenylmethane
347
10.6.7
Valporic Acid
347
10.6.8
Terpenoids
348
10.6.9
Fused Benzene—Cycloalkane Compounds
352
10.6.10
Nitrogenous Compounds
352
10.6.11
Halogenated Compounds
355
10.7
Summary
357
References
358
Chapter
11
QM/MM Studies of Cytochrome P450 Systems:
Application to Drug Metabolism
366
Richard Lonsdale
,
Jeremy
N.
Harvey and
Adrian
J
. Mutholland
11.1
Introduction
366
11.2
CYPs and Drug Metabolism
369
11.3
Quantum Mechanical/Molecular Mechanical
(QM/MM) Methods
371
Contents xiii
11.4 QM/MM
Studies of CYPs
374
11.4.1
Catalytic Cycle of CYP101 (CYP 450cam)
374
11.4.2
Hydroxylation of Camphor by CYP 450cam
380
11.4.3
Compound I Reactivity and Selectivity
383
11.4.4
Aromatic Hydroxylation
387
11.4.5
Other QM/MM Studies of CYPs
391
11.5
Conclusions
393
References
394
Chapter
12
Mechanism and Function of Tryptophan and Indoleamine
Dioxygenases
400
Sarah J. Thackray, Igor Efimov, Emma Lloyd Raven
and Christopher G. Mowat
12.1
Introduction
400
12.2
Biological and Physiological Function
of Indoleamine Dioxygenase and
Tryptophan Dioxygenase
401
12.3
Structures of TDO and
IDO
404
12.3.1
Comparison of Overall Structure
404
12.3.2
Active Site Environments
406
12.4
Turnover and Inhibition
408
12.4.1
Steady State Kinetics
408
12.4.2
Inhibition of TDO and
IDO
410
12.5
Catalytic Cycle
411
12.5.1
Formation of the Active Ternary Complex
411
12.5.2
Electrochemical Control of Substrate
Reactivity
413
12.5.3
Heme
Coordination Environment
414
12.5.4
Mechanism of Oxygen Insertion
418
12.6
Summary and Conclusions
421
References
422
Subject Index
427
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| id | DE-604.BV040374373 |
| illustrated | Illustrated |
| indexdate | 2024-07-10T00:22:47Z |
| institution | BVB |
| isbn | 9781849731812 1849731810 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-025227918 |
| oclc_num | 812242426 |
| open_access_boolean | |
| owner | DE-91G DE-BY-TUM DE-355 DE-BY-UBR |
| owner_facet | DE-91G DE-BY-TUM DE-355 DE-BY-UBR |
| physical | XIII, 448 S. : Ill., graph. Darst. 24 cm |
| publishDate | 2011 |
| publishDateSearch | 2011 |
| publishDateSort | 2011 |
| publisher | RSC Publ. |
| record_format | marc |
| spelling | Iron-containing enzymes versatile catalysts of hydroxylation reactions in nature ed. by Sam P. de Visser ... iron-containing Cambridge RSC Publ. 2011 XIII, 448 S. : Ill., graph. Darst. 24 cm txt rdacontent n rdamedia nc rdacarrier Katalyse (DE-588)4029921-1 gnd rswk-swf Eisenkomplexe (DE-588)4222910-8 gnd rswk-swf Enzym (DE-588)4014988-2 gnd rswk-swf Metalloenzymes Enzym (DE-588)4014988-2 s Eisenkomplexe (DE-588)4222910-8 s Katalyse (DE-588)4029921-1 s DE-604 Visser, Sam P. de Sonstige oth Digitalisierung UB Regensburg - ADAM Catalogue Enrichment application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025227918&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | Iron-containing enzymes versatile catalysts of hydroxylation reactions in nature Katalyse (DE-588)4029921-1 gnd Eisenkomplexe (DE-588)4222910-8 gnd Enzym (DE-588)4014988-2 gnd |
| subject_GND | (DE-588)4029921-1 (DE-588)4222910-8 (DE-588)4014988-2 |
| title | Iron-containing enzymes versatile catalysts of hydroxylation reactions in nature |
| title_alt | iron-containing |
| title_auth | Iron-containing enzymes versatile catalysts of hydroxylation reactions in nature |
| title_exact_search | Iron-containing enzymes versatile catalysts of hydroxylation reactions in nature |
| title_full | Iron-containing enzymes versatile catalysts of hydroxylation reactions in nature ed. by Sam P. de Visser ... |
| title_fullStr | Iron-containing enzymes versatile catalysts of hydroxylation reactions in nature ed. by Sam P. de Visser ... |
| title_full_unstemmed | Iron-containing enzymes versatile catalysts of hydroxylation reactions in nature ed. by Sam P. de Visser ... |
| title_short | Iron-containing enzymes |
| title_sort | iron containing enzymes versatile catalysts of hydroxylation reactions in nature |
| title_sub | versatile catalysts of hydroxylation reactions in nature |
| topic | Katalyse (DE-588)4029921-1 gnd Eisenkomplexe (DE-588)4222910-8 gnd Enzym (DE-588)4014988-2 gnd |
| topic_facet | Katalyse Eisenkomplexe Enzym |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=025227918&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
| work_keys_str_mv | AT vissersampde ironcontainingenzymesversatilecatalystsofhydroxylationreactionsinnature AT vissersampde ironcontaining |