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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.
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