Handbook of flavoproteins. Vol. 2, Complex flavoproteins, dehydrogenase and physical methods /
The dynamic field of flavin and flavoprotein biochemistry has seen rapid advancement in recent years. This second book of thetwo volume set is focussing on complex flavoproteins and physical methods. Itgivesimportant new insights into the reaction mechanisms of flavin-containing enzymes and the role...
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| Other Authors: | , , |
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| Format: | Electronic eBook |
| Language: | English |
| Published: |
Berlin ; Boston :
De Gruyter,
[2013]
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| Subjects: | |
| Online Access: |
Full text (Emmanuel users only) |
MARC
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| 245 | 0 | 0 | |a Handbook of flavoproteins. |n Vol. 2, |p Complex flavoproteins, dehydrogenase and physical methods / |c edited by Russ Hille, Susan Miller, Bruce Palfey. |
| 264 | 1 | |a Berlin ; |a Boston : |b De Gruyter, |c [2013] | |
| 264 | 4 | |c ©2013 | |
| 300 | |a 1 online resource | ||
| 336 | |a text |b txt |2 rdacontent | ||
| 337 | |a computer |b c |2 rdamedia | ||
| 338 | |a online resource |b cr |2 rdacarrier | ||
| 504 | |a Includes bibliographical references and index. | ||
| 505 | 0 | |a Preface; 1 The reaction mechanisms of Groups A and B flavoprotein monooxygenases; 1.1 Introduction; 1.2 Enzymes acting upon aromatic substrates -- Group A; 1.2.1 Reactions catalyzed; 1.2.2 Protein structures; 1.2.3 Detailed mechanism of PHBH; 1.2.3.1 Reductive half-reaction; 1.2.3.2 Oxidative half-reaction; 1.2.3.3 Hydroxylation chemistry; 1.2.3.4 Summary; 1.3 Enzymes acting upon non-aromatic substrates -- Group B; 1.3.1 Reactions catalyzed and subclasses; 1.3.1.1 BVMOs; 1.3.1.2 FMOs; 1.3.1.3 NMOs; 1.3.1.4 YUCCAs; 1.3.2 Structural features; 1.4 References. | |
| 505 | 8 | |a 2 Flavin-dependent monooxygenases in siderophore biosynthesis2.1 Iron, an essential but scarce nutrient; 2.2 Siderophores; 2.2.1 Siderophores are important virulence factors; 2.2.2 Structural diversity of siderophores; 2.3 Flavin-dependent N-hydroxylating monooxygenases; 2.4 Catalytic cycle of NMOs; 2.4.1 Flavin reduction in NMOs; 2.4.2 Flavin oxidation in NMOs; 2.5 Three-dimensional structure of NMOs; 2.5.1 FAD-binding domain; 2.5.2 NADPH-binding domain; 2.5.3 L-Ornithine-binding domain; 2.6 The structural basis of substrate specifi city in NMOs. | |
| 505 | 8 | |a 2.7 Mechanism of stabilization of the C4a-hydroperoxyfl avin by NADP+2.8 Activation of NMOs by amino acid binding; 2.9 Unusual NMOs; 2.10 High-throughput screening assay to identify inhibitors of NMOs; 2.11 Conclusions; 2.12 References; 3 The flavin monooxygenases; 3.1 Introduction; 3.2 Occurrence and classifi cation; 3.2.1 Amino acid sequence motifs; 3.2.2 DNA screening; 3.3 Single-component fl avin monooxygenases; 3.3.1 Subclass A; 3.3.2 Subclass B; 3.3.3 Subclass C; 3.3.4 Subclass D; 3.3.5 Subclass E; 3.3.6 Subclass F; 3.4 Conclusions; 3.5 References. | |
| 505 | 8 | |a 4 Structure and catalytic mechanism of NADPH-cytochrome P450 oxidoreductase: a prototype of the difl avin oxidoreductase family of enzymes4.1 Introduction; 4.2 Properties of CYPOR fl avins; 4.3 Domain structure and function; 4.4 Membrane binding domain (MBD); 4.5 FMN domain; 4.6 Cytochrome P450 binding: role of the FMN domain and connecting domain; 4.7 FAD domain; 4.8 Mechanism of hydride transfer; 4.9 Interfl avin electron transfer; 4.10 FMN to heme electron transfer; 4.11 P450 catalysis; 4.12 Other CYPOR electron acceptors; 4.13 CYPOR domain movement and control of electron transfer. | |
| 505 | 8 | |a 4.14 Physiological functions of CYPOR and effects of CYPOR defi ciency4.15 Human CYPOR defi ciency (PORD); 4.16 Contribution of CYPOR to inter-individual variation in human drug metabolism; 4.17 Unanswered questions and future directions; 4.18 References; 5 The xanthine oxidoreductase enzyme family: xanthine dehydrogenase, xanthine oxidase, and aldehyde oxidase; 5.1 Introduction; 5.2 Overall structures; 5.3 Reaction mechanism; 5.4 Electron transfer from the molybdenum center to other redox-active centers; 5.5 Reaction of FAD with NAD+ or molecular oxygen. | |
| 520 | |a The dynamic field of flavin and flavoprotein biochemistry has seen rapid advancement in recent years. This second book of thetwo volume set is focussing on complex flavoproteins and physical methods. Itgivesimportant new insights into the reaction mechanisms of flavin-containing enzymes and the role of flavoproteins in cell signalling pathways, and isan essential reference for all researchers in biochemistry, chemistry, photochemistry and photophysics working on flavoenzymes. | ||
| 588 | 0 | |a Print version record. | |
| 650 | 0 | |a Flavoproteins. | |
| 650 | 0 | |a Oxidoreductases. | |
| 650 | 2 | |a Flavoproteins | |
| 650 | 2 | |a Oxidoreductases | |
| 700 | 1 | |a Hille, Russ. | |
| 700 | 1 | |a Miller, Susan, |d 1955 December 21- |1 https://id.oclc.org/worldcat/entity/E39PCjwfrthrfxB9MQq9BKmQmb | |
| 700 | 1 | |a Palfey, Bruce. | |
| 758 | |i has work: |a Volume 2 Handbook of flavoproteins Complex flavoproteins, dehydrogenase and physical methods (Text) |1 https://id.oclc.org/worldcat/entity/E39PCGBGD67Wf7YVmKjwqt3Kbb |4 https://id.oclc.org/worldcat/ontology/hasWork | ||
| 776 | 0 | 8 | |i Print version: |a Miller, Susan. |t Handbook of Flavoproteins : Volume 2 Complex Flavoproteins, Dehydrogenases and Physical Methods. |d Berlin : De Gruyter, ©2013 |z 9783110298284 |
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