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Flavin-Based Catalysis: Principles and Applications [Kõva köide]

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  • Formaat: Hardback, 336 pages, kõrgus x laius x paksus: 244x170x23 mm, kaal: 794 g
  • Ilmumisaeg: 14-Jul-2021
  • Kirjastus: Blackwell Verlag GmbH
  • ISBN-10: 3527348344
  • ISBN-13: 9783527348343
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Flavin-Based Catalysis: Principles and ApplicationsSuurem pilt
  • Formaat: Hardback, 336 pages, kõrgus x laius x paksus: 244x170x23 mm, kaal: 794 g
  • Ilmumisaeg: 14-Jul-2021
  • Kirjastus: Blackwell Verlag GmbH
  • ISBN-10: 3527348344
  • ISBN-13: 9783527348343
Teised raamatud teemal:
Püsilink: https://www.kriso.ee/db/9783527348343.html
Märksõnad:

The book gives a unique overview of this rapidly developing research field, presenting structures and properties of flavin derivatives as well as their proven application as bioinspired catalysts in various organocatalytic, biocatalytic, and photocatalytic reactions.

Preface xi
1 Structure and Properties of Flavins
1(28)
Tetiana Pavlovska
Radek Cibulka
1.1 Introduction and History of Flavins Discovery
1(2)
1.2 The Structure of the Flavins and Their Derivatives
3(2)
1.3 The Acid-Base and Redox Properties of Flavin Derivatives
5(7)
1.3.1 Selected Chemical Reduction and Oxidation Reactions
9(3)
1.4 The Reactions of Flavin Derivatives with Nucleophiles and Electrophiles
12(4)
1.5 Noncovalent Interactions of Flavin Derivatives
16(3)
1.6 Conclusions
19(10)
References
20(9)
2 Natural Flavins: Occurrence, Role, and Noncanonical Chemistry
29(38)
Jeroen Drenth
Marco W. Fraaije
2.1 Introduction
29(1)
2.2 Flavin Biosynthesis
30(1)
2.3 Covalently Bound Flavin Cofactors
31(8)
2.3.1 Types and Occurrence of Covalent Protein-Flavin Bonds
33(1)
2.3.2 The Mechanisms of Protein-Flavin Bond Formation
34(1)
2.3.2.1 Formation of the Protein-Flavin Bond at the C8a Position
34(2)
2.3.2.2 Formation of the 6-S-Cysteinyl-Flavin Bond
36(1)
2.3.2.3 Formation of the Phosphoester Threonyl-FMN Bond
36(2)
2.3.3 The Function of Covalent Flavinylation
38(1)
2.3.3.1 Redox Potential
38(1)
2.3.3.2 Structural Integrity and Holoenzyme Lifetime
39(1)
2.4 Naturally Occurring Riboflavin Analogues and Modified Flavins - Roles and Occurrence
39(6)
2.4.1 6-Hydroxy and 7-Methyl-8-Hydroxyflavins
39(2)
2.4.2 6-(3'-(R)-Myristyl)Flavin Mononucleotide
41(1)
2.4.3 Chizoflavins
41(1)
2.4.4 7-Hydroxymethyl and 8-Hydroxymethyl Riboflavin
41(1)
2.4.5 Plant Root Iron Uptake Cofactors
41(1)
2.4.6 Roseoflavin - An Antimicrobial Flavin Analogue
42(1)
2.4.7 8-Formyl Flavins
42(1)
2.4.8 Prenyl-FMN
43(1)
2.4.9 Artificial Cofactors and Novel Catalytic Activity
44(1)
2.5 N5-substrate and N5-oxygen Adducts
45(4)
2.5.1 Redox-neutral Covalent Catalysis
45(2)
2.5.2 N5-oxygen Adducts
47(2)
2.6 F420 - A Natural Deazaflavin
49(3)
2.6.1 Structure and Properties of F420
49(1)
2.6.2 Physiological Functions of F420
49(1)
2.6.3 F420 Biosynthesis
50(2)
2.6.4 F420-dependent Enzymes in Biocatalysis
52(1)
2.7 Conclusion
52(15)
References
53(14)
3 Spectral Properties of Flavins
67(30)
Marek Sikorski
Igor Khmelinskii
Ewa Sikorska
3.1 Introduction
67(2)
3.2 Flavin Derivatives in Organic Solvents
69(8)
3.2.1 Spectroscopy and Photophysics
69(6)
3.2.2 Photooxygenation
75(1)
3.2.3 Solvent Effect
75(2)
3.2.4 Photostability
77(1)
3.3 Flavin Derivatives in Water
77(11)
3.3.1 Flavin (Isoalloxazine) Type of Compounds
77(3)
3.3.2 Alloxazine-type Compounds
80(3)
3.3.3 Deazaalloxazine-type Compounds
83(2)
3.3.4 Deazaisoalloxazine-type Compounds
85(3)
3.4 Conclusions
88(9)
References
88(9)
4 Modes of Flavin-Based Catalysis
97(28)
Radek Cibulka
Marco W. Fraaije
4.1 Introduction
97(3)
4.2 Modes of Catalysis
100(10)
4.2.1 Reactions Based on the Direct Transformation of a Substrate by Flavin
101(1)
4.2.1.1 Organocatalysis and Biocatalysis in the Absence of Light
101(4)
4.2.1.2 Flavin-Based Catalysis in an Excited State
105(4)
4.2.2 Flavin Catalyst-Activated Reactive Species Used to Transform the Substrate
109(1)
4.3 Flavin Catalysts Regeneration
110(3)
4.4 Development of New Flavin-Based Catalytic Methodologies
113(12)
References
115(10)
5 Organocatalytic Monooxygenations
125(20)
Hiroki Lida
Yasushi Imada
5.1 Introduction
125(2)
5.2 Catalytic Oxygenation with Hydrogen Peroxide
127(4)
5.3 Catalytic Oxygenation with Molecular Oxygen
131(6)
5.4 Asymmetric Oxygenation
137(2)
5.5 Conclusion and Outlook
139(6)
References
140(5)
6 Flavin-Based Supramolecular and Coupled Catalytic Systems
145(24)
Hiroki Lida
Yasushi Imada
6.1 Introduction
145(1)
6.2 Flavin-Based Supramolecular Systems
146(10)
6.2.1 Supramolecular Systems for Control of Reactivity
146(9)
6.2.2 Supramolecular Systems for the Control of Stereoselectivity
155(1)
6.3 Flavin-Based Coupled Catalytic Systems
156(8)
6.4 Conclusion and Outlook
164(5)
References
164(5)
7 Flavoprotein Monooxygenases and Halogenases
169(32)
Caroline E. Paul
Alice Guarneri
Willem J.H. van Berkel
7.1 Introduction
169(4)
7.1.1 Reaction Mechanisms of Flavoprotein Monooxygenases
169(1)
7.1.2 Classification of Flavoprotein Monooxygenases
170(3)
7.1.3 Oxygenation Reactions
173(1)
7.2 Types of Reactions Catalyzed by Group A-H Enzymes
173(12)
7.2.1 Group A Reactions
173(2)
7.2.2 Group B Reactions
175(3)
7.2.3 Group C Reactions
178(1)
7.2.4 Group D Reactions
179(3)
7.2.5 Group E Reactions
182(1)
7.2.6 Group F Reactions
183(1)
7.2.7 Group G and H Reactions
184(1)
7.3 Further Considerations for Biocatalyst Applications
185(1)
7.4 Conclusions and Outlook
186(15)
References
186(15)
8 Flavoprotein-dependent Bioreduction
201(24)
Helen S. Toogood
Nigel S. Scrutton
8.1 Introduction
201(1)
8.2 Flavoprotein Reductases
202(5)
8.2.1 Old Yellow Enzymes
202(1)
8.2.2 Enoate Reductases
203(1)
8.2.3 Nitroreductases
204(1)
8.2.4 Deazaflavin Oxidoreductase
205(1)
8.2.5 Geranylgeranyl Reductase
206(1)
8.2.6 NADPH-dependent Quinone Reductases
206(1)
8.3 Asymmetric Alkene Reduction: Biotechnological Applications
207(8)
8.3.1 Supply of Reducing Equivalents
207(2)
8.3.2 Industrially Relevant Chiral Products
209(1)
8.3.2.1 Aldehydes and Ketones
209(2)
8.3.2.2 Carboxylic Acids and Esters
211(1)
8.3.2.3 Alcohols, Diols, and Phenolics
212(1)
8.3.2.4 Monoterpenoids and Lactones
213(1)
8.3.2.5 Other Industrially Useful Compounds
214(1)
8.4 Conclusion
215(10)
References
216(9)
9 Flavoprotein Oxidases
225(20)
Daniel Ouedraogo
Giovanni Gadda
9.1 Introduction
225(1)
9.2 General Features
226(2)
9.3 Catalytic Cycle and Mechanism of Substrate Oxidation
228(1)
9.4 C--O Bond Oxidation
229(6)
9.4.1 S-Hydroxymethylfurfural Oxidase
230(1)
9.4.2 Phanerochaete chrysosporium Alcohol Oxidase
230(2)
9.4.3 Glycolate Oxidase
232(1)
9.4.4 Glucose Oxidase
232(2)
9.4.5 Pyranose Oxidase
234(1)
9.4.6 Cholesterol Oxidase
235(1)
9.5 C--N Bond Oxidation - D-Amino Acid Oxidase
235(1)
9.6 C--S Bond Oxidation - Sulfhydryl Oxidases
236(1)
9.7 C--C Bond Oxidation - NADH Oxidase
237(1)
9.8 Conclusions
238(7)
Acknowledgments
240(1)
Funding
240(1)
References
240(5)
10 Benzylic Photooxidation by Flavins
245(20)
Beiyi Cheng
Burkhard Konig
10.1 Introduction
245(1)
10.2 Flavins in Oxidations
246(12)
10.2.1 Early Examples of Flavin Oxidation
246(2)
10.2.2 More Recent Examples of Flavin Photooxidation
248(1)
10.2.2.1 The Oxidation of Benzylic Alcohols
248(7)
10.2.2.2 The Oxidation of Benzylic C--H Bonds
255(2)
10.2.2.3 The Oxidation of Benzylic Amines
257(1)
10.3 Conclusion
258(7)
References
260(5)
11 New Applications of Flavin Photocatalysis
265(28)
Eva Svobodova
Radek Cibulka
11.1 Introduction
265(1)
11.2 Transformations Involving Oxidation of Heteroatoms
266(6)
11.2.1 Sulfoxidation
267(3)
11.2.2 Esterifkation
270(2)
11.3 [ 2 + 2] Cycloaddition and Cycloelimination
272(4)
11.3.1 [ 2 + 2] Cycloaddition
273(1)
11.3.2 [ 2 + 2] Cycloelimination
274(2)
11.4 Transformations Involving Isomerization and Oxidative Cyclization
276(3)
11.4.1 E-Z Isomerization
276(2)
11.4.2 Cyclization Toward Coumarins
278(1)
11.4.3 Cyclization Toward Benzothiazoles
278(1)
11.5 Transformations Involving Decarboxylation
279(3)
11.6 Other Applications of Flavin-Based Oxidative Photocatalysis
282(1)
11.6.1 Chlorination
282(1)
11.6.2 Demethylation
283(1)
11.7 Reductive Photocatalysis
283(2)
11.8 Conclusions and Perspectives
285(8)
References
286(7)
12 Light-Driven Flavin-Based Biocatalysis
293(1)
Dana Grosheva
Todd K. Hyster
12.1 Introduction
293(2)
12.2 Native Light-Driven Enzymes
295(4)
12.3 Enzymes with Light-Driven Promiscuous Activities
299(6)
12.4 Synergistic Photoenzymatic Catalysis
305(4)
12.5 Conclusions and Outlook
309(6)
Acknowledgments
310(1)
References
310(5)
Index 315
Radek Cibulka is Full Professor and Head of the Department of Organic Chemistry at the University of Chemistry and Technology (UCT) in Prague, Czech Republic. He has authored over 60 scientific publications and received numerous scientific awards, including "Alfred Bader Prize", which is given by the Czech Chemical Society and the Alfred Bader Foundation to young scientists under 35 years. His research interests lie in chemistry and photochemistry of flavins and their application in organo- and photocatalysis.