Characterization, Properties and Applications

Tracey Rouault

ISBN 10: 3110478501 / ISBN 13: 9783110478501

Published by De Gruyter, 2017

About this Item

Druck auf Anfrage Neuware - Printed after ordering - 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.

Seller Inventory # 9783110478501

Bibliographic Details

• Title: Characterization, Properties and Applications
• Publisher: De Gruyter
• Publication Date: 2017
• Language: English
• ISBN 10: 3110478501
• ISBN 13: 9783110478501
• Binding: Buch
• Edition: 2nd Edition
• Condition: Neu
• Dimensions: 246W x 175H x 31D millimeters 246 millimeters width by 175 millimeters height by 31 millimeters depth
• Weight: 963 grams

About this title

Synopsis

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.

About the Author

Tracey Rouault, NIH Bethesda, Maryland, USA