Multi-copper oxidases /:
The biological activation of dioxygen is a key reaction in biological systems. Enzymes involved in direct oxygen activation are oxidases and oxygenases. Multi-copper oxidases are an important class of oxidases reducing dioxygen in a four-electron reduction to water with concomitant one-electron oxid...
Gespeichert in:
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| Format: | Elektronisch E-Book |
| Sprache: | English |
| Veröffentlicht: |
Singapore ; River Edge, NJ :
World Scientific,
©1997.
|
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Zusammenfassung: | The biological activation of dioxygen is a key reaction in biological systems. Enzymes involved in direct oxygen activation are oxidases and oxygenases. Multi-copper oxidases are an important class of oxidases reducing dioxygen in a four-electron reduction to water with concomitant one-electron oxidation of the reducing substrate. The progress in the characterization and understanding of the structure and function of these enzymes has advanced so tremendously over the last ten years that the publication of a book documenting these achievements has been overdue. Especially the recent discovery of a key role of the FET3 protein of Saccharomyces cerevisae, a multi-copper oxidase, in iron metabolism of this eukaryote has underpinned the function of the plasma multi-copper oxidase ceruloplasmin in vetebrate iron transport. The lately determined x-ray structure of human ceruloplasmin confirms its close structural relatedness to the plant multi-copper oxidases ascorbate oxidase and laccase and due to strong amino-acid sequence similarities has allowed to construct a useful model of the more distantly related blood-clotting factor VIII. This book contains review articles from experts in the field, dealing with modern spectroscopy, enzyme kinetics, bioinorganic chemistry, x-ray crystallography, electron transfer reactions, molecular biology, medical aspects and potential industrial applications of the three main members of multi-copper oxidases, i.e., laccase, ascorbate oxidase and ceruloplasmin. |
| Beschreibung: | 1 online resource (x, 465 pages) : illustrations (some color) |
| Bibliographie: | Includes bibliographical references and index. |
| ISBN: | 9789812830081 9812830081 |
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| 505 | 0 | |a Ch. 1. Early and more recent history in the research on multi-copper oxidases / Bo. G. Malmstrom -- ch. 2. Spatial structures of ascorbate oxidase, laccase and related proteins: Implications for the catalytic mechanism / A. Messerschmidt -- ch. 3. The structure of human ceruloplasmin at 3.1 A resolution / P.F. Lindley [and others] -- ch. 4. Spectroscopy of multi-copper oxidases / E.I. Solomon, T.E. Machonkin and U.M. Sundaram -- ch. 5. Bioinorganic chemistry of laccase / D.R. McMillin and M.K. Eggleston -- ch. 6. Kinetic studies on polyporus and tree laccases / B. Reinhammar -- ch. 7. Fungal laccases: Role in delignification and possible industrial applications / M. Smith, C.F. Thurston and D.A. Wood -- ch. 8. Spectroscopy of cucumber ascorbate oxidase and fungal laccase / T. Sakurai and S. Suzuki -- ch. 9. Biological function and enzyme kinetics of ascorbate oxidase / L. Avigliano and A. Finazzi-Agro -- ch. 10. The biology of human ceruloplasmin / Z. Leah Harris, H. Morita and J.D. Gitlin -- ch. 11. Molecular properties of ceruloplasmin from different species / L. Calabrese and G. Musci -- ch. 12. Electron transfer reactions in multi-copper oxidases / O. Farver and I. Pecht -- ch. 13. Redox properties of blue multi-copper oxidases / P.M.H. Kroneck -- ch. 14. Model compounds for multi-copper oxidases / P. Chaudhuri -- ch. 15. [symbol]Hg-derivatives of laccase and ascorbate oxidase: A hyperfine spectroscopic study / T. Butz and W. Troger. | |
| 520 | |a The biological activation of dioxygen is a key reaction in biological systems. Enzymes involved in direct oxygen activation are oxidases and oxygenases. Multi-copper oxidases are an important class of oxidases reducing dioxygen in a four-electron reduction to water with concomitant one-electron oxidation of the reducing substrate. The progress in the characterization and understanding of the structure and function of these enzymes has advanced so tremendously over the last ten years that the publication of a book documenting these achievements has been overdue. Especially the recent discovery of a key role of the FET3 protein of Saccharomyces cerevisae, a multi-copper oxidase, in iron metabolism of this eukaryote has underpinned the function of the plasma multi-copper oxidase ceruloplasmin in vetebrate iron transport. The lately determined x-ray structure of human ceruloplasmin confirms its close structural relatedness to the plant multi-copper oxidases ascorbate oxidase and laccase and due to strong amino-acid sequence similarities has allowed to construct a useful model of the more distantly related blood-clotting factor VIII. This book contains review articles from experts in the field, dealing with modern spectroscopy, enzyme kinetics, bioinorganic chemistry, x-ray crystallography, electron transfer reactions, molecular biology, medical aspects and potential industrial applications of the three main members of multi-copper oxidases, i.e., laccase, ascorbate oxidase and ceruloplasmin. | ||
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| contents | Ch. 1. Early and more recent history in the research on multi-copper oxidases / Bo. G. Malmstrom -- ch. 2. Spatial structures of ascorbate oxidase, laccase and related proteins: Implications for the catalytic mechanism / A. Messerschmidt -- ch. 3. The structure of human ceruloplasmin at 3.1 A resolution / P.F. Lindley [and others] -- ch. 4. Spectroscopy of multi-copper oxidases / E.I. Solomon, T.E. Machonkin and U.M. Sundaram -- ch. 5. Bioinorganic chemistry of laccase / D.R. McMillin and M.K. Eggleston -- ch. 6. Kinetic studies on polyporus and tree laccases / B. Reinhammar -- ch. 7. Fungal laccases: Role in delignification and possible industrial applications / M. Smith, C.F. Thurston and D.A. Wood -- ch. 8. Spectroscopy of cucumber ascorbate oxidase and fungal laccase / T. Sakurai and S. Suzuki -- ch. 9. Biological function and enzyme kinetics of ascorbate oxidase / L. Avigliano and A. Finazzi-Agro -- ch. 10. The biology of human ceruloplasmin / Z. Leah Harris, H. Morita and J.D. Gitlin -- ch. 11. Molecular properties of ceruloplasmin from different species / L. Calabrese and G. Musci -- ch. 12. Electron transfer reactions in multi-copper oxidases / O. Farver and I. Pecht -- ch. 13. Redox properties of blue multi-copper oxidases / P.M.H. Kroneck -- ch. 14. Model compounds for multi-copper oxidases / P. Chaudhuri -- ch. 15. [symbol]Hg-derivatives of laccase and ascorbate oxidase: A hyperfine spectroscopic study / T. Butz and W. Troger. |
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| discipline | Biologie |
| format | Electronic eBook |
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| id | ZDB-4-EBA-ocn827945010 |
| illustrated | Illustrated |
| indexdate | 2024-11-27T13:25:11Z |
| institution | BVB |
| isbn | 9789812830081 9812830081 |
| language | English |
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| publisher | World Scientific, |
| record_format | marc |
| spelling | Multi-copper oxidases / editor, Albrecht Messerschmidt. Singapore ; River Edge, NJ : World Scientific, ©1997. 1 online resource (x, 465 pages) : illustrations (some color) text txt rdacontent computer c rdamedia online resource cr rdacarrier Includes bibliographical references and index. Print version record. Ch. 1. Early and more recent history in the research on multi-copper oxidases / Bo. G. Malmstrom -- ch. 2. Spatial structures of ascorbate oxidase, laccase and related proteins: Implications for the catalytic mechanism / A. Messerschmidt -- ch. 3. The structure of human ceruloplasmin at 3.1 A resolution / P.F. Lindley [and others] -- ch. 4. Spectroscopy of multi-copper oxidases / E.I. Solomon, T.E. Machonkin and U.M. Sundaram -- ch. 5. Bioinorganic chemistry of laccase / D.R. McMillin and M.K. Eggleston -- ch. 6. Kinetic studies on polyporus and tree laccases / B. Reinhammar -- ch. 7. Fungal laccases: Role in delignification and possible industrial applications / M. Smith, C.F. Thurston and D.A. Wood -- ch. 8. Spectroscopy of cucumber ascorbate oxidase and fungal laccase / T. Sakurai and S. Suzuki -- ch. 9. Biological function and enzyme kinetics of ascorbate oxidase / L. Avigliano and A. Finazzi-Agro -- ch. 10. The biology of human ceruloplasmin / Z. Leah Harris, H. Morita and J.D. Gitlin -- ch. 11. Molecular properties of ceruloplasmin from different species / L. Calabrese and G. Musci -- ch. 12. Electron transfer reactions in multi-copper oxidases / O. Farver and I. Pecht -- ch. 13. Redox properties of blue multi-copper oxidases / P.M.H. Kroneck -- ch. 14. Model compounds for multi-copper oxidases / P. Chaudhuri -- ch. 15. [symbol]Hg-derivatives of laccase and ascorbate oxidase: A hyperfine spectroscopic study / T. Butz and W. Troger. The biological activation of dioxygen is a key reaction in biological systems. Enzymes involved in direct oxygen activation are oxidases and oxygenases. Multi-copper oxidases are an important class of oxidases reducing dioxygen in a four-electron reduction to water with concomitant one-electron oxidation of the reducing substrate. The progress in the characterization and understanding of the structure and function of these enzymes has advanced so tremendously over the last ten years that the publication of a book documenting these achievements has been overdue. Especially the recent discovery of a key role of the FET3 protein of Saccharomyces cerevisae, a multi-copper oxidase, in iron metabolism of this eukaryote has underpinned the function of the plasma multi-copper oxidase ceruloplasmin in vetebrate iron transport. The lately determined x-ray structure of human ceruloplasmin confirms its close structural relatedness to the plant multi-copper oxidases ascorbate oxidase and laccase and due to strong amino-acid sequence similarities has allowed to construct a useful model of the more distantly related blood-clotting factor VIII. This book contains review articles from experts in the field, dealing with modern spectroscopy, enzyme kinetics, bioinorganic chemistry, x-ray crystallography, electron transfer reactions, molecular biology, medical aspects and potential industrial applications of the three main members of multi-copper oxidases, i.e., laccase, ascorbate oxidase and ceruloplasmin. Oxidases. http://id.loc.gov/authorities/subjects/sh85096306 Copper proteins. http://id.loc.gov/authorities/subjects/sh85032388 Oxydases. Cuproprotéines. SCIENCE Life Sciences Biochemistry. bisacsh Copper proteins fast Oxidases fast Aufsatzsammlung gnd Kupferkomplexe gnd Oxidasen gnd http://d-nb.info/gnd/4173016-1 Messerschmidt, Albrecht. Print version: Multi-copper oxidases. Singapore ; River Edge, NJ : World Scientific, ©1997 9810227116 (OCoLC)37453759 FWS01 ZDB-4-EBA FWS_PDA_EBA https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&AN=512546 Volltext |
| spellingShingle | Multi-copper oxidases / Ch. 1. Early and more recent history in the research on multi-copper oxidases / Bo. G. Malmstrom -- ch. 2. Spatial structures of ascorbate oxidase, laccase and related proteins: Implications for the catalytic mechanism / A. Messerschmidt -- ch. 3. The structure of human ceruloplasmin at 3.1 A resolution / P.F. Lindley [and others] -- ch. 4. Spectroscopy of multi-copper oxidases / E.I. Solomon, T.E. Machonkin and U.M. Sundaram -- ch. 5. Bioinorganic chemistry of laccase / D.R. McMillin and M.K. Eggleston -- ch. 6. Kinetic studies on polyporus and tree laccases / B. Reinhammar -- ch. 7. Fungal laccases: Role in delignification and possible industrial applications / M. Smith, C.F. Thurston and D.A. Wood -- ch. 8. Spectroscopy of cucumber ascorbate oxidase and fungal laccase / T. Sakurai and S. Suzuki -- ch. 9. Biological function and enzyme kinetics of ascorbate oxidase / L. Avigliano and A. Finazzi-Agro -- ch. 10. The biology of human ceruloplasmin / Z. Leah Harris, H. Morita and J.D. Gitlin -- ch. 11. Molecular properties of ceruloplasmin from different species / L. Calabrese and G. Musci -- ch. 12. Electron transfer reactions in multi-copper oxidases / O. Farver and I. Pecht -- ch. 13. Redox properties of blue multi-copper oxidases / P.M.H. Kroneck -- ch. 14. Model compounds for multi-copper oxidases / P. Chaudhuri -- ch. 15. [symbol]Hg-derivatives of laccase and ascorbate oxidase: A hyperfine spectroscopic study / T. Butz and W. Troger. Oxidases. http://id.loc.gov/authorities/subjects/sh85096306 Copper proteins. http://id.loc.gov/authorities/subjects/sh85032388 Oxydases. Cuproprotéines. SCIENCE Life Sciences Biochemistry. bisacsh Copper proteins fast Oxidases fast Aufsatzsammlung gnd Kupferkomplexe gnd Oxidasen gnd http://d-nb.info/gnd/4173016-1 |
| subject_GND | http://id.loc.gov/authorities/subjects/sh85096306 http://id.loc.gov/authorities/subjects/sh85032388 http://d-nb.info/gnd/4173016-1 |
| title | Multi-copper oxidases / |
| title_auth | Multi-copper oxidases / |
| title_exact_search | Multi-copper oxidases / |
| title_full | Multi-copper oxidases / editor, Albrecht Messerschmidt. |
| title_fullStr | Multi-copper oxidases / editor, Albrecht Messerschmidt. |
| title_full_unstemmed | Multi-copper oxidases / editor, Albrecht Messerschmidt. |
| title_short | Multi-copper oxidases / |
| title_sort | multi copper oxidases |
| topic | Oxidases. http://id.loc.gov/authorities/subjects/sh85096306 Copper proteins. http://id.loc.gov/authorities/subjects/sh85032388 Oxydases. Cuproprotéines. SCIENCE Life Sciences Biochemistry. bisacsh Copper proteins fast Oxidases fast Aufsatzsammlung gnd Kupferkomplexe gnd Oxidasen gnd http://d-nb.info/gnd/4173016-1 |
| topic_facet | Oxidases. Copper proteins. Oxydases. Cuproprotéines. SCIENCE Life Sciences Biochemistry. Copper proteins Oxidases Aufsatzsammlung Kupferkomplexe Oxidasen |
| url | https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&AN=512546 |
| work_keys_str_mv | AT messerschmidtalbrecht multicopperoxidases |