Summary
Iron-sulfur clusters in proteins are now recognized as among the main types of electron-transferring groups in biological systems, besides heme and flavins. Recent developments have brought forth a better understanding about the ways the protein environment modulates the potential of the cluster by placing the cluster in a more or less hydrophobic surrounding. Refinement in models, extensive studies on the kinetics of electron transfer (e.g. by measurement of the electronic spin lattice relaxation time) and the introduction of novel spectroscopic methods (EXAFS, magnetic CD and others) in the elucidation of structures in various systems are among the main developments. Other advances include EPR studies of the spatial orientation of Fe−S centers in complex membraneous systems (e.g. in mitochondria) and the recent elucidation of the nature of center X in photosystem I by Mössbauer-spectroscopy. Mössbauer studies have also been described on a number of Fe−S proteins (nitrogenase, aconitase, some ferredoxins, etc.) and revealed the existence of novel structures that enlarged the number of known basic units of Fe−S centers. These advances include: 1. the discovery of a novel non-heme Fe-protein (called desulforedoxin) of the rebredoxin type, 2. the elucidation of the nitrogenase Fe−S centers and the nitrogenase cofactor and 3. the discovery of a three-iron cluster in several enzymes and some ferredoxins. The latter 3-Fe cluster seems capable of being converted into a classical 4-Fe cluster under appropriate conditions, a phenomenon that plays a role in activation-deactivation of some enzymes (e.g. aconitase). It is now recognized that some iron-sulfur clusters may be involved in systems devoided of any oxydation-reduction reaction and may act as sensors of the surrounding redox potential, triggering the activation/deactivation of an enzyme (cf. e.g. aconitase).
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Dreyer, JL. Iron-sulfur proteins: Recent developments in the field. Experientia 38, 521–529 (1982). https://doi.org/10.1007/BF02327030
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DOI: https://doi.org/10.1007/BF02327030