Iron-Sulfur Clusters in Chemistry and Biology. / Volume 1, : Characterization, Properties and Applications / / ed. by Tracey Rouault.

• Superior document: Title is part of eBook package: De Gruyter DG Plus eBook-Package 2017
• MitwirkendeR: Andrade, Susana L. A.,; Bonomi, Francesco,; Booker, Squire J.,; Chakrabarti, Mrinmoy,; Crack, Jason C.,; Dodd, Erin L.,; Einsle, Oliver,; Fontecilla-Camps, Juan C.,; Guo, Yisong,; Hendrich, Michael P.,; Hille, Russ,; Hu, Yilin,; Ichiye, Toshiko,; Jarrett, Joseph T.,; Lanz, Nicholas D.,; Le Brun, Nick E.,; Li, Jikun,; Lindahl, Paul A.,; Nicolet, Yvain,; Noodleman, Louis,; Petasis, Doros T.,; Ribbe, Markus,; Rouault, Tracey A.,; Sickerman, Nathaniel S.,; Spatzal, Thomas,; Thomson, Andrew J.,
• TeilnehmendeR: Andrade, Susana L.A.; Bonomi, Francesco.; Booker, Squire.; Chakrabarti, Mrinmoy.; Crack, Jason.; Dodd, Erin.; Einsle, Oliver.; Fontecilla, Juan.; Guo, Yisong.; Hendrich, Michael.; Hille, Russ.; Hu, Yilin.; Ichiye, Toshiko.; Jarrett, Joe .; Jikun, Li.; Lanz, Nicholas D.; Le Brun, Nick.; Lindahl, Paul.; Louis, Noodleman.; Nicolet, Yvain.; Petasis, Doros T.; Ribbe, Markus.; Spatzal, Thomas.; Thomson, Andrew.; Wenge, Han.
• HerausgeberIn: Rouault, Tracey,
• Place / Publishing House: Berlin ;, Boston : : De Gruyter, , [2017]; ©2017
• Year of Publication: 2017
• Edition: 2. Aufl.
• Language: English
• Series: Iron-Sulfur Clusters in Chemistry and Biology ; Volume 1
• Physical Description: 1 online resource (XV, 447 p.)

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.

Table of Contents

Frontmatter -- Preface -- Tracey A. Rouault biography -- Contents -- List of contributing authors -- 1. Iron-sulfur proteins: a historical perspective -- 2. Chemistry of iron-sulfur clusters -- 3. From the quantum chemistry of iron-sulfur clusters to redox energetics and reaction pathways in metalloenzymes -- 4. Bioinorganic spectroscopy of iron sulfur proteins— an overview -- 5. Quantitative interpretation of EPR spectroscopy with applications for iron-sulfur proteins -- 6. The utility of Mössbauer spectroscopy in eukaryotic cell biology and animal physiology -- 7. The interstitial carbide of the nitrogenase M-cluster: insertion pathway and possible function -- 8. The iron-molybdenum cofactor of nitrogenase -- 9. Biotin synthase: a role for iron-sulfur clusters in the radical-mediated generation of carbon-sulfur bonds -- 10. Molybdenum-containing iron-sulfur enzymes -- 11. The role of iron-sulfur clusters in the biosynthesis of the lipoyl cofactor -- 12. Iron-sulfur clusters and molecular oxygen: function, adaptation, degradation, and repair -- 13. Reactivity of iron-sulfur clusters with nitric oxide -- Index