Clostridial iron-sulphur proteins.

Iron-sulfur proteins are ubiquitous catalysts of a wide range of biological reactions, and are particularly abundant in clostridia which lack the ability to synthesize hemes. The development of research on these metalloproteins has therefore been strongly associated with biochemical investigations of clostridial metabolism. Major breakthroughs in the field, from the first isolation of an iron-sulfur protein in 1962, to the recent determination of an Fe-hydrogenase structure, have been made with clostridia. These data, as well as others obtained through studies on clostridia, are transferable to many other bioenergetic machineries, due to the strong phylogenetic conservation of some important components. For instance, clear homologies exist between constituents of the anaerobic electron transfer chains in clostridia and aerobic respiratory chains. The contribution of iron-sulfur proteins to the biotechnological and medical significance of clostridia is also discussed. Structural and functional genomics are expected to bring forth a wealth of novel data on clostridia and iron-sulfur proteins.