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This volume on iron-sulfur proteins includes chapters that 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.
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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