Handbook of flavoproteins: Volume 1 oxidases, dehydrogenases and related systems
Gespeichert in:
| 1. Verfasser: | |
|---|---|
| Format: | Elektronisch E-Book |
| Sprache: | English |
| Veröffentlicht: |
Berlin
De Gruyter
2012
|
| Schlagworte: | |
| Online-Zugang: | FAW01 FAW02 Volltext |
| Beschreibung: | Print version record. - 5.3.2 Mechanisms of luciferase:flavin reductase coupled reactions |
| Beschreibung: | 1 online resource (372 pages) |
| ISBN: | 3110268914 9783110268911 |
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| 100 | 1 | |a Miller, Susan |d 1955 December 21- |e Verfasser |4 aut | |
| 245 | 1 | 0 | |a Handbook of flavoproteins |b Volume 1 oxidases, dehydrogenases and related systems |
| 264 | 1 | |a Berlin |b De Gruyter |c 2012 | |
| 300 | |a 1 online resource (372 pages) | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b c |2 rdamedia | ||
| 338 | |b cr |2 rdacarrier | ||
| 500 | |a Print version record. - 5.3.2 Mechanisms of luciferase:flavin reductase coupled reactions | ||
| 505 | 8 | |a Preface; 1 Berberine bridge enzyme and the family of bicovalent flavoenzymes; 1.1 Introduction; 1.2 The paradigm of bicovalent flavoenzymes: Berberine bridge enzyme (BBE) from Eschscholzia californica; 1.3 The family of BBE-like enzymes in the plant kingdom: how many and what for?; 1.4 The occurrence of BBE-like enzymes in fungi; 1.5 BBE-like enzymes in bacteria: oxidative power for the biosynthesis of antibiotics; 1.6 Conclusions; 1.7 Acknowledgments; 1.8 References; 2 PutA and proline metabolism; 2.1 Importance of proline metabolism; 2.2 Proline utilization A (PutA) proteins | |
| 505 | 8 | |a 2.3 Three-dimensional structures of PutA and PutA domains2.3.1 Structures of the catalytic domains of PutA; 2.3.2 Crystal structure of a minimalist PutA; 2.3.3 Solution structure of a trifunctional PutA and the role of the CTD; 2.4 Reaction kinetics of PutA; 2.4.1 Proline:ubiquinone oxidoreductase activity; 2.4.2 Substrate channeling; 2.5 DNA and membrane binding of trifunctional PutA; 2.5.1 DNA binding; 2.5.2 Membrane association; 2.6 PutA functional switching; 2.6.1 Redox-linked global conformational changes; 2.6.2 Local structural changes near the flavin | |
| 505 | 8 | |a 2.6.3 Residues important for functional switching2.7 Conclusions and future research directions; 2.8 Acknowledgements; 2.9 References; 3 Flavoenzymes involved in non-redox reactions; 3.1 Introduction; 3.2 Flavoenzymes for which flavin cofactors likely play redox-based catalytic roles; 3.2.1 Chorismate synthase; 3.2.2 4-Hydroxybutyryl-CoA dehydratase; 3.2.3 Polyunsaturated fatty acid isomerase; 3.2.4 4'-Phosphopantothenoylcysteine decarboxylase; 3.2.5 Other examples; 3.3 Flavoenzymes for which flavin cofactors likely play non-redox catalytic roles | |
| 505 | 8 | |a 3.3.1 Type 2 isopentenyl diphosphate isomerase3.3.2 UDP-galactopyranose mutase; 3.4 Flavoenzymes for which flavin cofactors play uncertain, but probably catalytic roles; 3.4.1 Lycopene cyclase; 3.4.2 Carotene cis-trans isomerase; 3.4.3 Fatty acid hydratase; 3.4.4 2-Haloacrylate hydratase; 3.5 Conclusions; 3.6 References; 4 Enzymes of FMN and FAD Metabolism; 4.1 Introduction; 4.2 Enzymes involved in the production of FMN and FAD in different organisms; 4.3 FMN and FAD metabolism in yeasts and mammals; 4.4 FMN and FAD metabolism in bacteria depends on a bifunctional enzyme | |
| 505 | 8 | |a 4.5 FMN and FAD metabolism in plants4.6 Conclusions and future research directions; 4.7 Acknowledgments; 4.8 References; 4.9 Abbreviations; 5 Mechanisms of bacterial luciferase and related flavin reductases; 5.1 Introduction; 5.2 Luciferase mechanism overview; 5.2.1 Mechanism of chemiexcitation; 5.2.2 Identity of primary excited state and emitter; 5.2.3 Multiple forms of 4a-hydroperoxy-FMNH intermediate II; 5.2.4 Aldehyde substrate inhibition; 5.3 Flavin reductases -- general remarks; 5.3.1 Mechanisms of flavin reductases in single-enzyme reactions | |
| 505 | 8 | |a The dynamic field of flavin and flavoprotein biochemistry has seen rapid advancement in recent years. Thisfirst book of thetwo volume set provides an overview of all aspects focussing on oxidases, dehydrogenases and related systems. Discussed arerecent developments in this field including those of large membrane-integral electron transfer complexes. It is an essential reference for all researchers in biochemistry, chemistry, photochemistry and photophysics working on flavoenzymes | |
| 650 | 4 | |a Bacterial proteins | |
| 650 | 4 | |a Flavins | |
| 650 | 4 | |a Oxidoreductases | |
| 650 | 7 | |a SCIENCE / Life Sciences / Biochemistry |2 bisacsh | |
| 650 | 7 | |a Flavoproteins |2 fast | |
| 650 | 4 | |a Flavoproteins | |
| 700 | 1 | |a Gregersen, Niels Henrik |d 1956- |e Sonstige |4 oth | |
| 700 | 1 | |a Rokita, Steven Edward |e Sonstige |4 oth | |
| 700 | 1 | |a Becker, Donald |e Sonstige |4 oth | |
| 700 | 1 | |a Hille, Russ |e Sonstige |4 oth | |
| 700 | 1 | |a Palfey, Bruce |e Sonstige |4 oth | |
| 700 | 1 | |a Binda, Claudia |e Sonstige |4 oth | |
| 700 | 1 | |a Ceccarelli, Eduardo |e Sonstige |4 oth | |
| 700 | 1 | |a Chaiyen, Pimchai |e Sonstige |4 oth | |
| 700 | 1 | |a Costa Filho, Antonio J. |e Sonstige |4 oth | |
| 700 | 1 | |a Daniel, Bastian |e Sonstige |4 oth | |
| 700 | 1 | |a Dully, Corinna |e Sonstige |4 oth | |
| 700 | 1 | |a Edmondson, D. E. |e Sonstige |4 oth | |
| 700 | 1 | |a Fitzpatrick, Paul |e Sonstige |4 oth | |
| 700 | 1 | |a Gadda, Giovanni |e Sonstige |4 oth | |
| 700 | 1 | |a Ghisla, S. |e Sonstige |4 oth | |
| 700 | 1 | |a Hemmi, Hisashi |e Sonstige |4 oth | |
| 700 | 1 | |a Jentoft Olsen, Rikke Katrine |e Sonstige |4 oth | |
| 700 | 1 | |a Kim, Jung-Ja |e Sonstige |4 oth | |
| 700 | 1 | |a Macheroux, Peter |e Sonstige |4 oth | |
| 700 | 1 | |a Mattevi, Andrea |e Sonstige |4 oth | |
| 700 | 1 | |a Medina, M. |e Sonstige |4 oth | |
| 700 | 1 | |a Nonato, Maria Cristina |e Sonstige |4 oth | |
| 700 | 1 | |a Schuman Jorns, Marilyn |e Sonstige |4 oth | |
| 700 | 1 | |a Tanner, John J. |e Sonstige |4 oth | |
| 776 | 0 | 8 | |i Erscheint auch als |n Druck-Ausgabe |a Miller, Susan |t Handbook of Flavoproteins : Volume 1 Oxidases, Dehydrogenases and Related Systems |
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Datensatz im Suchindex
| _version_ | 1804175395757490176 |
|---|---|
| any_adam_object | |
| author | Miller, Susan 1955 December 21- |
| author_facet | Miller, Susan 1955 December 21- |
| author_role | aut |
| author_sort | Miller, Susan 1955 December 21- |
| author_variant | s m sm |
| building | Verbundindex |
| bvnumber | BV043035779 |
| collection | ZDB-4-EBA |
| contents | Preface; 1 Berberine bridge enzyme and the family of bicovalent flavoenzymes; 1.1 Introduction; 1.2 The paradigm of bicovalent flavoenzymes: Berberine bridge enzyme (BBE) from Eschscholzia californica; 1.3 The family of BBE-like enzymes in the plant kingdom: how many and what for?; 1.4 The occurrence of BBE-like enzymes in fungi; 1.5 BBE-like enzymes in bacteria: oxidative power for the biosynthesis of antibiotics; 1.6 Conclusions; 1.7 Acknowledgments; 1.8 References; 2 PutA and proline metabolism; 2.1 Importance of proline metabolism; 2.2 Proline utilization A (PutA) proteins 2.3 Three-dimensional structures of PutA and PutA domains2.3.1 Structures of the catalytic domains of PutA; 2.3.2 Crystal structure of a minimalist PutA; 2.3.3 Solution structure of a trifunctional PutA and the role of the CTD; 2.4 Reaction kinetics of PutA; 2.4.1 Proline:ubiquinone oxidoreductase activity; 2.4.2 Substrate channeling; 2.5 DNA and membrane binding of trifunctional PutA; 2.5.1 DNA binding; 2.5.2 Membrane association; 2.6 PutA functional switching; 2.6.1 Redox-linked global conformational changes; 2.6.2 Local structural changes near the flavin 2.6.3 Residues important for functional switching2.7 Conclusions and future research directions; 2.8 Acknowledgements; 2.9 References; 3 Flavoenzymes involved in non-redox reactions; 3.1 Introduction; 3.2 Flavoenzymes for which flavin cofactors likely play redox-based catalytic roles; 3.2.1 Chorismate synthase; 3.2.2 4-Hydroxybutyryl-CoA dehydratase; 3.2.3 Polyunsaturated fatty acid isomerase; 3.2.4 4'-Phosphopantothenoylcysteine decarboxylase; 3.2.5 Other examples; 3.3 Flavoenzymes for which flavin cofactors likely play non-redox catalytic roles 3.3.1 Type 2 isopentenyl diphosphate isomerase3.3.2 UDP-galactopyranose mutase; 3.4 Flavoenzymes for which flavin cofactors play uncertain, but probably catalytic roles; 3.4.1 Lycopene cyclase; 3.4.2 Carotene cis-trans isomerase; 3.4.3 Fatty acid hydratase; 3.4.4 2-Haloacrylate hydratase; 3.5 Conclusions; 3.6 References; 4 Enzymes of FMN and FAD Metabolism; 4.1 Introduction; 4.2 Enzymes involved in the production of FMN and FAD in different organisms; 4.3 FMN and FAD metabolism in yeasts and mammals; 4.4 FMN and FAD metabolism in bacteria depends on a bifunctional enzyme 4.5 FMN and FAD metabolism in plants4.6 Conclusions and future research directions; 4.7 Acknowledgments; 4.8 References; 4.9 Abbreviations; 5 Mechanisms of bacterial luciferase and related flavin reductases; 5.1 Introduction; 5.2 Luciferase mechanism overview; 5.2.1 Mechanism of chemiexcitation; 5.2.2 Identity of primary excited state and emitter; 5.2.3 Multiple forms of 4a-hydroperoxy-FMNH intermediate II; 5.2.4 Aldehyde substrate inhibition; 5.3 Flavin reductases -- general remarks; 5.3.1 Mechanisms of flavin reductases in single-enzyme reactions The dynamic field of flavin and flavoprotein biochemistry has seen rapid advancement in recent years. Thisfirst book of thetwo volume set provides an overview of all aspects focussing on oxidases, dehydrogenases and related systems. Discussed arerecent developments in this field including those of large membrane-integral electron transfer complexes. It is an essential reference for all researchers in biochemistry, chemistry, photochemistry and photophysics working on flavoenzymes |
| ctrlnum | (OCoLC)829462145 (DE-599)BVBBV043035779 |
| dewey-full | 572.791 |
| dewey-hundreds | 500 - Natural sciences and mathematics |
| dewey-ones | 572 - Biochemistry |
| dewey-raw | 572.791 |
| dewey-search | 572.791 |
| dewey-sort | 3572.791 |
| dewey-tens | 570 - Biology |
| discipline | Biologie |
| format | Electronic eBook |
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| id | DE-604.BV043035779 |
| illustrated | Not Illustrated |
| indexdate | 2024-07-10T07:15:37Z |
| institution | BVB |
| isbn | 3110268914 9783110268911 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-028460429 |
| oclc_num | 829462145 |
| open_access_boolean | |
| owner | DE-1046 DE-1047 |
| owner_facet | DE-1046 DE-1047 |
| physical | 1 online resource (372 pages) |
| psigel | ZDB-4-EBA ZDB-4-EBA FAW_PDA_EBA |
| publishDate | 2012 |
| publishDateSearch | 2012 |
| publishDateSort | 2012 |
| publisher | De Gruyter |
| record_format | marc |
| spelling | Miller, Susan 1955 December 21- Verfasser aut Handbook of flavoproteins Volume 1 oxidases, dehydrogenases and related systems Berlin De Gruyter 2012 1 online resource (372 pages) txt rdacontent c rdamedia cr rdacarrier Print version record. - 5.3.2 Mechanisms of luciferase:flavin reductase coupled reactions Preface; 1 Berberine bridge enzyme and the family of bicovalent flavoenzymes; 1.1 Introduction; 1.2 The paradigm of bicovalent flavoenzymes: Berberine bridge enzyme (BBE) from Eschscholzia californica; 1.3 The family of BBE-like enzymes in the plant kingdom: how many and what for?; 1.4 The occurrence of BBE-like enzymes in fungi; 1.5 BBE-like enzymes in bacteria: oxidative power for the biosynthesis of antibiotics; 1.6 Conclusions; 1.7 Acknowledgments; 1.8 References; 2 PutA and proline metabolism; 2.1 Importance of proline metabolism; 2.2 Proline utilization A (PutA) proteins 2.3 Three-dimensional structures of PutA and PutA domains2.3.1 Structures of the catalytic domains of PutA; 2.3.2 Crystal structure of a minimalist PutA; 2.3.3 Solution structure of a trifunctional PutA and the role of the CTD; 2.4 Reaction kinetics of PutA; 2.4.1 Proline:ubiquinone oxidoreductase activity; 2.4.2 Substrate channeling; 2.5 DNA and membrane binding of trifunctional PutA; 2.5.1 DNA binding; 2.5.2 Membrane association; 2.6 PutA functional switching; 2.6.1 Redox-linked global conformational changes; 2.6.2 Local structural changes near the flavin 2.6.3 Residues important for functional switching2.7 Conclusions and future research directions; 2.8 Acknowledgements; 2.9 References; 3 Flavoenzymes involved in non-redox reactions; 3.1 Introduction; 3.2 Flavoenzymes for which flavin cofactors likely play redox-based catalytic roles; 3.2.1 Chorismate synthase; 3.2.2 4-Hydroxybutyryl-CoA dehydratase; 3.2.3 Polyunsaturated fatty acid isomerase; 3.2.4 4'-Phosphopantothenoylcysteine decarboxylase; 3.2.5 Other examples; 3.3 Flavoenzymes for which flavin cofactors likely play non-redox catalytic roles 3.3.1 Type 2 isopentenyl diphosphate isomerase3.3.2 UDP-galactopyranose mutase; 3.4 Flavoenzymes for which flavin cofactors play uncertain, but probably catalytic roles; 3.4.1 Lycopene cyclase; 3.4.2 Carotene cis-trans isomerase; 3.4.3 Fatty acid hydratase; 3.4.4 2-Haloacrylate hydratase; 3.5 Conclusions; 3.6 References; 4 Enzymes of FMN and FAD Metabolism; 4.1 Introduction; 4.2 Enzymes involved in the production of FMN and FAD in different organisms; 4.3 FMN and FAD metabolism in yeasts and mammals; 4.4 FMN and FAD metabolism in bacteria depends on a bifunctional enzyme 4.5 FMN and FAD metabolism in plants4.6 Conclusions and future research directions; 4.7 Acknowledgments; 4.8 References; 4.9 Abbreviations; 5 Mechanisms of bacterial luciferase and related flavin reductases; 5.1 Introduction; 5.2 Luciferase mechanism overview; 5.2.1 Mechanism of chemiexcitation; 5.2.2 Identity of primary excited state and emitter; 5.2.3 Multiple forms of 4a-hydroperoxy-FMNH intermediate II; 5.2.4 Aldehyde substrate inhibition; 5.3 Flavin reductases -- general remarks; 5.3.1 Mechanisms of flavin reductases in single-enzyme reactions The dynamic field of flavin and flavoprotein biochemistry has seen rapid advancement in recent years. Thisfirst book of thetwo volume set provides an overview of all aspects focussing on oxidases, dehydrogenases and related systems. Discussed arerecent developments in this field including those of large membrane-integral electron transfer complexes. It is an essential reference for all researchers in biochemistry, chemistry, photochemistry and photophysics working on flavoenzymes Bacterial proteins Flavins Oxidoreductases SCIENCE / Life Sciences / Biochemistry bisacsh Flavoproteins fast Flavoproteins Gregersen, Niels Henrik 1956- Sonstige oth Rokita, Steven Edward Sonstige oth Becker, Donald Sonstige oth Hille, Russ Sonstige oth Palfey, Bruce Sonstige oth Binda, Claudia Sonstige oth Ceccarelli, Eduardo Sonstige oth Chaiyen, Pimchai Sonstige oth Costa Filho, Antonio J. Sonstige oth Daniel, Bastian Sonstige oth Dully, Corinna Sonstige oth Edmondson, D. E. Sonstige oth Fitzpatrick, Paul Sonstige oth Gadda, Giovanni Sonstige oth Ghisla, S. Sonstige oth Hemmi, Hisashi Sonstige oth Jentoft Olsen, Rikke Katrine Sonstige oth Kim, Jung-Ja Sonstige oth Macheroux, Peter Sonstige oth Mattevi, Andrea Sonstige oth Medina, M. Sonstige oth Nonato, Maria Cristina Sonstige oth Schuman Jorns, Marilyn Sonstige oth Tanner, John J. Sonstige oth Erscheint auch als Druck-Ausgabe Miller, Susan Handbook of Flavoproteins : Volume 1 Oxidases, Dehydrogenases and Related Systems http://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&db=nlabk&AN=543960 Aggregator Volltext |
| spellingShingle | Miller, Susan 1955 December 21- Handbook of flavoproteins Volume 1 oxidases, dehydrogenases and related systems Preface; 1 Berberine bridge enzyme and the family of bicovalent flavoenzymes; 1.1 Introduction; 1.2 The paradigm of bicovalent flavoenzymes: Berberine bridge enzyme (BBE) from Eschscholzia californica; 1.3 The family of BBE-like enzymes in the plant kingdom: how many and what for?; 1.4 The occurrence of BBE-like enzymes in fungi; 1.5 BBE-like enzymes in bacteria: oxidative power for the biosynthesis of antibiotics; 1.6 Conclusions; 1.7 Acknowledgments; 1.8 References; 2 PutA and proline metabolism; 2.1 Importance of proline metabolism; 2.2 Proline utilization A (PutA) proteins 2.3 Three-dimensional structures of PutA and PutA domains2.3.1 Structures of the catalytic domains of PutA; 2.3.2 Crystal structure of a minimalist PutA; 2.3.3 Solution structure of a trifunctional PutA and the role of the CTD; 2.4 Reaction kinetics of PutA; 2.4.1 Proline:ubiquinone oxidoreductase activity; 2.4.2 Substrate channeling; 2.5 DNA and membrane binding of trifunctional PutA; 2.5.1 DNA binding; 2.5.2 Membrane association; 2.6 PutA functional switching; 2.6.1 Redox-linked global conformational changes; 2.6.2 Local structural changes near the flavin 2.6.3 Residues important for functional switching2.7 Conclusions and future research directions; 2.8 Acknowledgements; 2.9 References; 3 Flavoenzymes involved in non-redox reactions; 3.1 Introduction; 3.2 Flavoenzymes for which flavin cofactors likely play redox-based catalytic roles; 3.2.1 Chorismate synthase; 3.2.2 4-Hydroxybutyryl-CoA dehydratase; 3.2.3 Polyunsaturated fatty acid isomerase; 3.2.4 4'-Phosphopantothenoylcysteine decarboxylase; 3.2.5 Other examples; 3.3 Flavoenzymes for which flavin cofactors likely play non-redox catalytic roles 3.3.1 Type 2 isopentenyl diphosphate isomerase3.3.2 UDP-galactopyranose mutase; 3.4 Flavoenzymes for which flavin cofactors play uncertain, but probably catalytic roles; 3.4.1 Lycopene cyclase; 3.4.2 Carotene cis-trans isomerase; 3.4.3 Fatty acid hydratase; 3.4.4 2-Haloacrylate hydratase; 3.5 Conclusions; 3.6 References; 4 Enzymes of FMN and FAD Metabolism; 4.1 Introduction; 4.2 Enzymes involved in the production of FMN and FAD in different organisms; 4.3 FMN and FAD metabolism in yeasts and mammals; 4.4 FMN and FAD metabolism in bacteria depends on a bifunctional enzyme 4.5 FMN and FAD metabolism in plants4.6 Conclusions and future research directions; 4.7 Acknowledgments; 4.8 References; 4.9 Abbreviations; 5 Mechanisms of bacterial luciferase and related flavin reductases; 5.1 Introduction; 5.2 Luciferase mechanism overview; 5.2.1 Mechanism of chemiexcitation; 5.2.2 Identity of primary excited state and emitter; 5.2.3 Multiple forms of 4a-hydroperoxy-FMNH intermediate II; 5.2.4 Aldehyde substrate inhibition; 5.3 Flavin reductases -- general remarks; 5.3.1 Mechanisms of flavin reductases in single-enzyme reactions The dynamic field of flavin and flavoprotein biochemistry has seen rapid advancement in recent years. Thisfirst book of thetwo volume set provides an overview of all aspects focussing on oxidases, dehydrogenases and related systems. Discussed arerecent developments in this field including those of large membrane-integral electron transfer complexes. It is an essential reference for all researchers in biochemistry, chemistry, photochemistry and photophysics working on flavoenzymes Bacterial proteins Flavins Oxidoreductases SCIENCE / Life Sciences / Biochemistry bisacsh Flavoproteins fast Flavoproteins |
| title | Handbook of flavoproteins Volume 1 oxidases, dehydrogenases and related systems |
| title_auth | Handbook of flavoproteins Volume 1 oxidases, dehydrogenases and related systems |
| title_exact_search | Handbook of flavoproteins Volume 1 oxidases, dehydrogenases and related systems |
| title_full | Handbook of flavoproteins Volume 1 oxidases, dehydrogenases and related systems |
| title_fullStr | Handbook of flavoproteins Volume 1 oxidases, dehydrogenases and related systems |
| title_full_unstemmed | Handbook of flavoproteins Volume 1 oxidases, dehydrogenases and related systems |
| title_short | Handbook of flavoproteins |
| title_sort | handbook of flavoproteins volume 1 oxidases dehydrogenases and related systems |
| title_sub | Volume 1 oxidases, dehydrogenases and related systems |
| topic | Bacterial proteins Flavins Oxidoreductases SCIENCE / Life Sciences / Biochemistry bisacsh Flavoproteins fast Flavoproteins |
| topic_facet | Bacterial proteins Flavins Oxidoreductases SCIENCE / Life Sciences / Biochemistry Flavoproteins |
| url | http://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&db=nlabk&AN=543960 |
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