Iron-Sulfur Clusters in Chemistry and Biology / / ed. by Tracey Rouault.
This volume on iron-sulfur proteins includes chapters that describe the initial discovery of iron-sulfur proteins in the 1960s to elucidation of the roles of iron sulfur clusters as prosthetic groups of enzymes, such as the citric acid cycle enzyme, aconitase, and numerous other proteins, ranging fr...
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Iron-Sulfur Clusters in Chemistry and Biology / ed. by Tracey Rouault. Berlin ; Boston : De Gruyter, [2014] ©2014 1 online resource (648 p.) text txt rdacontent computer c rdamedia online resource cr rdacarrier text file PDF rda Frontmatter -- Preface -- Tracey A. Rouault biography -- Contents -- Contributing authors -- 1. Iron-sulfur proteins: a historical perspective -- 2. Chemistry of iron-sulfur clusters -- 3. Quantitative interpretation of EPR spectroscopy with applications for iron-sulfur proteins -- 4. The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology -- 5. The interstitial carbide of the nitrogenase M-cluster: insertion pathway and possible function -- 6. The iron-molybdenum cofactor of nitrogenase -- 7. Biotin synthase: a role for iron-sulfur clusters in the radical-mediated generation of carbon-sulfur bonds -- 8. Molybdenum-containing iron-sulfur enzymes -- 9. The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor -- 10. Iron-sulfur clusters and molecular oxygen: function, adaptation, degradation, and repair -- 11. A retrospective on the discovery of [Fe-S] cluster biosynthetic machineries in Azotobacter vinelandii -- 12. A stress-responsive Fe-S cluster biogenesis system in bacteria – the suf operon of Gammaproteobacteria -- 13. Sensing the cellular Fe-S cluster demand: a structural, functional, and phylogenetic overview of Escherichia coli IscR -- 14. Fe-S assembly in Gram-positive bacteria -- 15. Fe-S cluster assembly and regulation in yeast -- 16. The role of Fe-S clusters in regulation of yeast iron homeostasis -- 17. Biogenesis of Fe-S proteins in mammals -- 18. Iron-sulfur proteins and human diseases -- 19. Connecting the biosynthesis of the molybdenum cofactor, Fe-S clusters, and tRNA thiolation in humans -- 20. Iron-sulfur proteins and genome stability -- 21. Eukaryotic iron-sulfur protein biogenesis and its role in maintaining genomic integrity -- 22. Iron-sulfur cluster assembly in plants -- 23. Origin and evolution of Fe-S proteins and enzymes -- Index restricted access http://purl.org/coar/access_right/c_16ec online access with authorization star This volume on iron-sulfur proteins includes chapters that describe the initial discovery of iron-sulfur proteins in the 1960s to elucidation of the roles of iron sulfur clusters as prosthetic groups of enzymes, such as the citric acid cycle enzyme, aconitase, and numerous other proteins, ranging from nitrogenase to DNA repair proteins. The capacity of iron sulfur clusters to accept and delocalize single electrons is explained by basic chemical principles, which illustrate why iron sulfur proteins are uniquely suitable for electron transport and other activities. Techniques used for detection and stabilization of iron-sulfur clusters, including EPR and Mossbauer spectroscopies, are discussed because they are important for characterizing unrecognized and elusive iron sulfur proteins. Recent insights into how nitrogenase works have arisen from multiple advances, described here, including studies of high-resolution crystal structures. Numerous chapters discuss how microbes, plants, and animals synthesize these complex prosthetic groups, and why it is important to understand the chemistry and biogenesis of iron sulfur proteins. In addition to their vital importance in mitochondrial respiration, numerous iron sulfur proteins are important in maintenance of DNA integrity. Multiple rare human diseases with different clinical presentations are caused by mutations of genes in the iron sulfur cluster biogenesis pathway. Understanding iron sulfur proteins is important for understanding a rapidly expanding group of metabolic pathways important in all kingdoms of life, and for understanding processes ranging from nitrogen fixation to human disease. Issued also in print. Mode of access: Internet via World Wide Web. In English. Description based on online resource; title from PDF title page (publisher's Web site, viewed 01. Dez 2022) Iron-sulfur proteins. SCIENCE / Life Sciences / Molecular Biology. bisacsh Adams, Michael W. W., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Adams, Michael W.W., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Andrade, Susana L. A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Andrade, Susana L.A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Bonomi, Francesco, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Booker, Squire J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Booker, Squire, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Boyd, Eric S., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Broderick, Joan B. , contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Broderick, Joan B., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Chakrabarti, Mrinmoy, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dancis, Andrew, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dancis, Andy , contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dean, Dennis R., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dean, Dennis, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dos Santos, Patricia C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Dos Santos, Patricia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Einsle, Oliver, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Fontecilla, Juan, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Fontecilla-Camps, Juan C., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Gari, Kerstin, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hendrich, Michael P., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hendrich, Michael, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hille, Russ, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Hu, Yilin, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ichiye, Toshiko, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jarrett, Joe , contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Jarrett, Joseph T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kiley, Patricia J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Kiley, Patricia, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lanz, Nicholas D., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Leimkuhler, Silke, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Leimkühler, Silke, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lill, Roland, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lindahl, Paul A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Lindahl, Paul, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Mettert, Erin L., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Nicolet, Yvain, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Outten, Caryn , contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Outten, Caryn E., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Outten, F. Wayne, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Outten, Wayne, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Pain, Debkumar, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Perna, Nicole T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Petasis, Doros T., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Peters, John , contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Peters, John W., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ribbe, Markus, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rouault, Tracey A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Rouault, Tracey, editor. edt http://id.loc.gov/vocabulary/relators/edt Schut, Gerrit J., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Shepard, Eric M., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Spatzal, Thomas, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tong, Wing Hang, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Tong, Wing-Hang, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Uzarska, Marta A., contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Uzarska, Marta, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Wohlschlegel, James , contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Wohlschlegel, James, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Ye, Hong, contributor. ctb https://id.loc.gov/vocabulary/relators/ctb Title is part of eBook package: De Gruyter DGBA Backlist Complete English Language 2000-2014 PART1 9783110238570 Title is part of eBook package: De Gruyter DGBA Backlist Physical Sciences 2000-2014 (EN) 9783110238518 Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences 2000 - 2014 9783110637915 ZDB-23-GML Title is part of eBook package: De Gruyter EBOOK PACKAGE Chemistry, Materials Sc, Biol, Geosc 2014 9783110369601 ZDB-23-DCM Title is part of eBook package: De Gruyter EBOOK PACKAGE Complete Package 2014 9783110369526 ZDB-23-DGG print 9783110308327 https://doi.org/10.1515/9783110308426 https://www.degruyter.com/isbn/9783110308426 Cover https://www.degruyter.com/document/cover/isbn/9783110308426/original |
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English |
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Adams, Michael W. W., Adams, Michael W. W., Adams, Michael W.W., Adams, Michael W.W., Andrade, Susana L. A., Andrade, Susana L. A., Andrade, Susana L.A., Andrade, Susana L.A., Bonomi, Francesco, Bonomi, Francesco, Booker, Squire J., Booker, Squire J., Booker, Squire, Booker, Squire, Boyd, Eric S., Boyd, Eric S., Broderick, Joan B. , Broderick, Joan B. , Broderick, Joan B., Broderick, Joan B., Chakrabarti, Mrinmoy, Chakrabarti, Mrinmoy, Dancis, Andrew, Dancis, Andrew, Dancis, Andy , Dancis, Andy , Dean, Dennis R., Dean, Dennis R., Dean, Dennis, Dean, Dennis, Dos Santos, Patricia C., Dos Santos, Patricia C., Dos Santos, Patricia, Dos Santos, Patricia, Einsle, Oliver, Einsle, Oliver, Fontecilla, Juan, Fontecilla, Juan, Fontecilla-Camps, Juan C., Fontecilla-Camps, Juan C., Gari, Kerstin, Gari, Kerstin, Hendrich, Michael P., Hendrich, Michael P., Hendrich, Michael, Hendrich, Michael, Hille, Russ, Hille, Russ, Hu, Yilin, Hu, Yilin, Ichiye, Toshiko, Ichiye, Toshiko, Jarrett, Joe , Jarrett, Joe , Jarrett, Joseph T., Jarrett, Joseph T., Kiley, Patricia J., Kiley, Patricia J., Kiley, Patricia, Kiley, Patricia, Lanz, Nicholas D., Lanz, Nicholas D., Leimkuhler, Silke, Leimkuhler, Silke, Leimkühler, Silke, Leimkühler, Silke, Lill, Roland, Lill, Roland, Lindahl, Paul A., Lindahl, Paul A., Lindahl, Paul, Lindahl, Paul, Mettert, Erin L., Mettert, Erin L., Nicolet, Yvain, Nicolet, Yvain, Outten, Caryn , Outten, Caryn , Outten, Caryn E., Outten, Caryn E., Outten, F. Wayne, Outten, F. Wayne, Outten, Wayne, Outten, Wayne, Pain, Debkumar, Pain, Debkumar, Perna, Nicole T., Perna, Nicole T., Petasis, Doros T., Petasis, Doros T., Peters, John , Peters, John , Peters, John W., Peters, John W., Ribbe, Markus, Ribbe, Markus, Rouault, Tracey A., Rouault, Tracey A., Rouault, Tracey, Rouault, Tracey, Schut, Gerrit J., Schut, Gerrit J., Shepard, Eric M., Shepard, Eric M., Spatzal, Thomas, Spatzal, Thomas, Tong, Wing Hang, Tong, Wing Hang, Tong, Wing-Hang, Tong, Wing-Hang, Uzarska, Marta A., Uzarska, Marta A., Uzarska, Marta, Uzarska, Marta, Wohlschlegel, James , Wohlschlegel, James , Wohlschlegel, James, Wohlschlegel, James, Ye, Hong, Ye, Hong, |
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Adams, Michael W. W., Adams, Michael W. W., Adams, Michael W.W., Adams, Michael W.W., Andrade, Susana L. A., Andrade, Susana L. A., Andrade, Susana L.A., Andrade, Susana L.A., Bonomi, Francesco, Bonomi, Francesco, Booker, Squire J., Booker, Squire J., Booker, Squire, Booker, Squire, Boyd, Eric S., Boyd, Eric S., Broderick, Joan B. , Broderick, Joan B. , Broderick, Joan B., Broderick, Joan B., Chakrabarti, Mrinmoy, Chakrabarti, Mrinmoy, Dancis, Andrew, Dancis, Andrew, Dancis, Andy , Dancis, Andy , Dean, Dennis R., Dean, Dennis R., Dean, Dennis, Dean, Dennis, Dos Santos, Patricia C., Dos Santos, Patricia C., Dos Santos, Patricia, Dos Santos, Patricia, Einsle, Oliver, Einsle, Oliver, Fontecilla, Juan, Fontecilla, Juan, Fontecilla-Camps, Juan C., Fontecilla-Camps, Juan C., Gari, Kerstin, Gari, Kerstin, Hendrich, Michael P., Hendrich, Michael P., Hendrich, Michael, Hendrich, Michael, Hille, Russ, Hille, Russ, Hu, Yilin, Hu, Yilin, Ichiye, Toshiko, Ichiye, Toshiko, Jarrett, Joe , Jarrett, Joe , Jarrett, Joseph T., Jarrett, Joseph T., Kiley, Patricia J., Kiley, Patricia J., Kiley, Patricia, Kiley, Patricia, Lanz, Nicholas D., Lanz, Nicholas D., Leimkuhler, Silke, Leimkuhler, Silke, Leimkühler, Silke, Leimkühler, Silke, Lill, Roland, Lill, Roland, Lindahl, Paul A., Lindahl, Paul A., Lindahl, Paul, Lindahl, Paul, Mettert, Erin L., Mettert, Erin L., Nicolet, Yvain, Nicolet, Yvain, Outten, Caryn , Outten, Caryn , Outten, Caryn E., Outten, Caryn E., Outten, F. Wayne, Outten, F. Wayne, Outten, Wayne, Outten, Wayne, Pain, Debkumar, Pain, Debkumar, Perna, Nicole T., Perna, Nicole T., Petasis, Doros T., Petasis, Doros T., Peters, John , Peters, John , Peters, John W., Peters, John W., Ribbe, Markus, Ribbe, Markus, Rouault, Tracey A., Rouault, Tracey A., Rouault, Tracey, Rouault, Tracey, Schut, Gerrit J., Schut, Gerrit J., Shepard, Eric M., Shepard, Eric M., Spatzal, Thomas, Spatzal, Thomas, Tong, Wing Hang, Tong, Wing Hang, Tong, Wing-Hang, Tong, Wing-Hang, Uzarska, Marta A., Uzarska, Marta A., Uzarska, Marta, Uzarska, Marta, Wohlschlegel, James , Wohlschlegel, James , Wohlschlegel, James, Wohlschlegel, James, Ye, Hong, Ye, Hong, |
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author_sort |
Adams, Michael W. W., |
title |
Iron-Sulfur Clusters in Chemistry and Biology / |
spellingShingle |
Iron-Sulfur Clusters in Chemistry and Biology / Frontmatter -- Preface -- Tracey A. Rouault biography -- Contents -- Contributing authors -- 1. Iron-sulfur proteins: a historical perspective -- 2. Chemistry of iron-sulfur clusters -- 3. Quantitative interpretation of EPR spectroscopy with applications for iron-sulfur proteins -- 4. The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology -- 5. The interstitial carbide of the nitrogenase M-cluster: insertion pathway and possible function -- 6. The iron-molybdenum cofactor of nitrogenase -- 7. Biotin synthase: a role for iron-sulfur clusters in the radical-mediated generation of carbon-sulfur bonds -- 8. Molybdenum-containing iron-sulfur enzymes -- 9. The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor -- 10. Iron-sulfur clusters and molecular oxygen: function, adaptation, degradation, and repair -- 11. A retrospective on the discovery of [Fe-S] cluster biosynthetic machineries in Azotobacter vinelandii -- 12. A stress-responsive Fe-S cluster biogenesis system in bacteria – the suf operon of Gammaproteobacteria -- 13. Sensing the cellular Fe-S cluster demand: a structural, functional, and phylogenetic overview of Escherichia coli IscR -- 14. Fe-S assembly in Gram-positive bacteria -- 15. Fe-S cluster assembly and regulation in yeast -- 16. The role of Fe-S clusters in regulation of yeast iron homeostasis -- 17. Biogenesis of Fe-S proteins in mammals -- 18. Iron-sulfur proteins and human diseases -- 19. Connecting the biosynthesis of the molybdenum cofactor, Fe-S clusters, and tRNA thiolation in humans -- 20. Iron-sulfur proteins and genome stability -- 21. Eukaryotic iron-sulfur protein biogenesis and its role in maintaining genomic integrity -- 22. Iron-sulfur cluster assembly in plants -- 23. Origin and evolution of Fe-S proteins and enzymes -- Index |
title_full |
Iron-Sulfur Clusters in Chemistry and Biology / ed. by Tracey Rouault. |
title_fullStr |
Iron-Sulfur Clusters in Chemistry and Biology / ed. by Tracey Rouault. |
title_full_unstemmed |
Iron-Sulfur Clusters in Chemistry and Biology / ed. by Tracey Rouault. |
title_auth |
Iron-Sulfur Clusters in Chemistry and Biology / |
title_alt |
Frontmatter -- Preface -- Tracey A. Rouault biography -- Contents -- Contributing authors -- 1. Iron-sulfur proteins: a historical perspective -- 2. Chemistry of iron-sulfur clusters -- 3. Quantitative interpretation of EPR spectroscopy with applications for iron-sulfur proteins -- 4. The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology -- 5. The interstitial carbide of the nitrogenase M-cluster: insertion pathway and possible function -- 6. The iron-molybdenum cofactor of nitrogenase -- 7. Biotin synthase: a role for iron-sulfur clusters in the radical-mediated generation of carbon-sulfur bonds -- 8. Molybdenum-containing iron-sulfur enzymes -- 9. The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor -- 10. Iron-sulfur clusters and molecular oxygen: function, adaptation, degradation, and repair -- 11. A retrospective on the discovery of [Fe-S] cluster biosynthetic machineries in Azotobacter vinelandii -- 12. A stress-responsive Fe-S cluster biogenesis system in bacteria – the suf operon of Gammaproteobacteria -- 13. Sensing the cellular Fe-S cluster demand: a structural, functional, and phylogenetic overview of Escherichia coli IscR -- 14. Fe-S assembly in Gram-positive bacteria -- 15. Fe-S cluster assembly and regulation in yeast -- 16. The role of Fe-S clusters in regulation of yeast iron homeostasis -- 17. Biogenesis of Fe-S proteins in mammals -- 18. Iron-sulfur proteins and human diseases -- 19. Connecting the biosynthesis of the molybdenum cofactor, Fe-S clusters, and tRNA thiolation in humans -- 20. Iron-sulfur proteins and genome stability -- 21. Eukaryotic iron-sulfur protein biogenesis and its role in maintaining genomic integrity -- 22. Iron-sulfur cluster assembly in plants -- 23. Origin and evolution of Fe-S proteins and enzymes -- Index |
title_new |
Iron-Sulfur Clusters in Chemistry and Biology / |
title_sort |
iron-sulfur clusters in chemistry and biology / |
publisher |
De Gruyter, |
publishDate |
2014 |
physical |
1 online resource (648 p.) Issued also in print. |
contents |
Frontmatter -- Preface -- Tracey A. Rouault biography -- Contents -- Contributing authors -- 1. Iron-sulfur proteins: a historical perspective -- 2. Chemistry of iron-sulfur clusters -- 3. Quantitative interpretation of EPR spectroscopy with applications for iron-sulfur proteins -- 4. The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology -- 5. The interstitial carbide of the nitrogenase M-cluster: insertion pathway and possible function -- 6. The iron-molybdenum cofactor of nitrogenase -- 7. Biotin synthase: a role for iron-sulfur clusters in the radical-mediated generation of carbon-sulfur bonds -- 8. Molybdenum-containing iron-sulfur enzymes -- 9. The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor -- 10. Iron-sulfur clusters and molecular oxygen: function, adaptation, degradation, and repair -- 11. A retrospective on the discovery of [Fe-S] cluster biosynthetic machineries in Azotobacter vinelandii -- 12. A stress-responsive Fe-S cluster biogenesis system in bacteria – the suf operon of Gammaproteobacteria -- 13. Sensing the cellular Fe-S cluster demand: a structural, functional, and phylogenetic overview of Escherichia coli IscR -- 14. Fe-S assembly in Gram-positive bacteria -- 15. Fe-S cluster assembly and regulation in yeast -- 16. The role of Fe-S clusters in regulation of yeast iron homeostasis -- 17. Biogenesis of Fe-S proteins in mammals -- 18. Iron-sulfur proteins and human diseases -- 19. Connecting the biosynthesis of the molybdenum cofactor, Fe-S clusters, and tRNA thiolation in humans -- 20. Iron-sulfur proteins and genome stability -- 21. Eukaryotic iron-sulfur protein biogenesis and its role in maintaining genomic integrity -- 22. Iron-sulfur cluster assembly in plants -- 23. Origin and evolution of Fe-S proteins and enzymes -- Index |
isbn |
9783110308426 9783110238570 9783110238518 9783110637915 9783110369601 9783110369526 9783110308327 |
url |
https://doi.org/10.1515/9783110308426 https://www.degruyter.com/isbn/9783110308426 https://www.degruyter.com/document/cover/isbn/9783110308426/original |
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Not Illustrated |
doi_str_mv |
10.1515/9783110308426 |
oclc_num |
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Title is part of eBook package: De Gruyter DGBA Backlist Complete English Language 2000-2014 PART1 Title is part of eBook package: De Gruyter DGBA Backlist Physical Sciences 2000-2014 (EN) Title is part of eBook package: De Gruyter DGBA Medicine and Life Sciences 2000 - 2014 Title is part of eBook package: De Gruyter EBOOK PACKAGE Chemistry, Materials Sc, Biol, Geosc 2014 Title is part of eBook package: De Gruyter EBOOK PACKAGE Complete Package 2014 |
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Iron-Sulfur Clusters in Chemistry and Biology / |
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Title is part of eBook package: De Gruyter DGBA Backlist Complete English Language 2000-2014 PART1 |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>12422nam a22014655i 4500</leader><controlfield tag="001">9783110308426</controlfield><controlfield tag="003">DE-B1597</controlfield><controlfield tag="005">20221201113901.0</controlfield><controlfield tag="006">m|||||o||d||||||||</controlfield><controlfield tag="007">cr || ||||||||</controlfield><controlfield tag="008">221201t20142014gw fo d z eng d</controlfield><datafield tag="019" ind1=" " ind2=" "><subfield code="a">(OCoLC)979753757</subfield></datafield><datafield tag="020" ind1=" " ind2=" "><subfield code="a">9783110308426</subfield></datafield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1515/9783110308426</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-B1597)207294</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(OCoLC)890071018</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-B1597</subfield><subfield code="b">eng</subfield><subfield code="c">DE-B1597</subfield><subfield code="e">rda</subfield></datafield><datafield tag="041" ind1="0" ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="044" ind1=" " ind2=" "><subfield code="a">gw</subfield><subfield code="c">DE</subfield></datafield><datafield tag="072" ind1=" " ind2="7"><subfield code="a">SCI049000</subfield><subfield code="2">bisacsh</subfield></datafield><datafield tag="245" ind1="0" ind2="0"><subfield code="a">Iron-Sulfur Clusters in Chemistry and Biology /</subfield><subfield code="c">ed. by Tracey Rouault.</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Berlin ;</subfield><subfield code="a">Boston : </subfield><subfield code="b">De Gruyter, </subfield><subfield code="c">[2014]</subfield></datafield><datafield tag="264" ind1=" " ind2="4"><subfield code="c">©2014</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">1 online resource (648 p.)</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">computer</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">online resource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="347" ind1=" " ind2=" "><subfield code="a">text file</subfield><subfield code="b">PDF</subfield><subfield code="2">rda</subfield></datafield><datafield tag="505" ind1="0" ind2="0"><subfield code="t">Frontmatter -- </subfield><subfield code="t">Preface -- </subfield><subfield code="t">Tracey A. Rouault biography -- </subfield><subfield code="t">Contents -- </subfield><subfield code="t">Contributing authors -- </subfield><subfield code="t">1. Iron-sulfur proteins: a historical perspective -- </subfield><subfield code="t">2. Chemistry of iron-sulfur clusters -- </subfield><subfield code="t">3. Quantitative interpretation of EPR spectroscopy with applications for iron-sulfur proteins -- </subfield><subfield code="t">4. The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology -- </subfield><subfield code="t">5. The interstitial carbide of the nitrogenase M-cluster: insertion pathway and possible function -- </subfield><subfield code="t">6. The iron-molybdenum cofactor of nitrogenase -- </subfield><subfield code="t">7. Biotin synthase: a role for iron-sulfur clusters in the radical-mediated generation of carbon-sulfur bonds -- </subfield><subfield code="t">8. Molybdenum-containing iron-sulfur enzymes -- </subfield><subfield code="t">9. The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor -- </subfield><subfield code="t">10. Iron-sulfur clusters and molecular oxygen: function, adaptation, degradation, and repair -- </subfield><subfield code="t">11. A retrospective on the discovery of [Fe-S] cluster biosynthetic machineries in Azotobacter vinelandii -- </subfield><subfield code="t">12. A stress-responsive Fe-S cluster biogenesis system in bacteria – the suf operon of Gammaproteobacteria -- </subfield><subfield code="t">13. Sensing the cellular Fe-S cluster demand: a structural, functional, and phylogenetic overview of Escherichia coli IscR -- </subfield><subfield code="t">14. Fe-S assembly in Gram-positive bacteria -- </subfield><subfield code="t">15. Fe-S cluster assembly and regulation in yeast -- </subfield><subfield code="t">16. The role of Fe-S clusters in regulation of yeast iron homeostasis -- </subfield><subfield code="t">17. Biogenesis of Fe-S proteins in mammals -- </subfield><subfield code="t">18. Iron-sulfur proteins and human diseases -- </subfield><subfield code="t">19. Connecting the biosynthesis of the molybdenum cofactor, Fe-S clusters, and tRNA thiolation in humans -- </subfield><subfield code="t">20. Iron-sulfur proteins and genome stability -- </subfield><subfield code="t">21. Eukaryotic iron-sulfur protein biogenesis and its role in maintaining genomic integrity -- </subfield><subfield code="t">22. Iron-sulfur cluster assembly in plants -- </subfield><subfield code="t">23. Origin and evolution of Fe-S proteins and enzymes -- </subfield><subfield code="t">Index</subfield></datafield><datafield tag="506" ind1="0" ind2=" "><subfield code="a">restricted access</subfield><subfield code="u">http://purl.org/coar/access_right/c_16ec</subfield><subfield code="f">online access with authorization</subfield><subfield code="2">star</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">This volume on iron-sulfur proteins includes chapters that describe the initial discovery of iron-sulfur proteins in the 1960s to elucidation of the roles of iron sulfur clusters as prosthetic groups of enzymes, such as the citric acid cycle enzyme, aconitase, and numerous other proteins, ranging from nitrogenase to DNA repair proteins. The capacity of iron sulfur clusters to accept and delocalize single electrons is explained by basic chemical principles, which illustrate why iron sulfur proteins are uniquely suitable for electron transport and other activities. Techniques used for detection and stabilization of iron-sulfur clusters, including EPR and Mossbauer spectroscopies, are discussed because they are important for characterizing unrecognized and elusive iron sulfur proteins. Recent insights into how nitrogenase works have arisen from multiple advances, described here, including studies of high-resolution crystal structures. Numerous chapters discuss how microbes, plants, and animals synthesize these complex prosthetic groups, and why it is important to understand the chemistry and biogenesis of iron sulfur proteins. In addition to their vital importance in mitochondrial respiration, numerous iron sulfur proteins are important in maintenance of DNA integrity. Multiple rare human diseases with different clinical presentations are caused by mutations of genes in the iron sulfur cluster biogenesis pathway. Understanding iron sulfur proteins is important for understanding a rapidly expanding group of metabolic pathways important in all kingdoms of life, and for understanding processes ranging from nitrogen fixation to human disease.</subfield></datafield><datafield tag="530" ind1=" " ind2=" "><subfield code="a">Issued also in print.</subfield></datafield><datafield tag="538" ind1=" " ind2=" "><subfield code="a">Mode of access: Internet via World Wide Web.</subfield></datafield><datafield tag="546" ind1=" " ind2=" "><subfield code="a">In English.</subfield></datafield><datafield tag="588" ind1="0" ind2=" "><subfield code="a">Description based on online resource; title from PDF title page (publisher's Web site, viewed 01. 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