Iron-sulfur proteins, present in animals, plants, and bacteria, are metalloproteins which play important roles as electron car
نویسنده
چکیده
Iron-sulfur clusters, functioning primarily as electron transfer agents, have important roles in biology, participating in plant photosynthesis, nitrogen fixation, steroid metabolism, and oxidative phosphorylation. Present in animals, plants, and bacteria, iron-sulfur clusters are found at the active sites of redox and catalytic proteins. Since the 1970s, metal sites in iron-sulfur proteins have been defined by X-ray crystallography and analogues of the iron-sulfur sites have been synthesized. Particular attention has been given to the synthesis of Fe4S4 analogues due to their unique electron transfer properties and wide occurrences in nature as active Fe4S4 protein sites. This paper will look at the developments of synthetic analogue complexes of the Fe4S4 sites in ironsulfur proteins and will highlight the electronic and geometric properties of isolated Fe4S4 analogues. Because of the weak field properties of thiolate and sulfide ligands, iron-sulfur clusters often exhibit tetrahedral site stereochemistry with tetragonal D2d distortion and high-spin d electron configurations in two oxidation states (Fe ). Properties of isolated Fe4S4 analogues to be briefly discussed include Mössbauer spectra, EPR spectra, ENDOR spectra, and X-ray crystal structures.
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تاریخ انتشار 2005