Research Areas

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Multiheme cytochromes, that are recognizably different from the monoheme c cytochromes, constitute a widespread class of proteins with essential functions in electron transfer and enzymatic catalysis. There is a high level of conservation of heme structural arrangement throughout various multi-heme cytochromes. However, the functional significance of such arrangements is not yet understood, and they possibly reflect favorable arrangements to tune heme–heme redox potential interactions and/or warrant very fast electron transfer. Understanding the significance of these heme structural motifs is crucial for the elucidation of the highly optimized properties of multiheme cytochromes which we are currently engaged in.

Interaction between heme centers has been smartly implemented by Nature in order to regulate different properties of multiheme cytochromes, thereby allowing them to perform a wide variety of functions. Our broad interest lies in unmasking the role played by heme-heme interaction in modulating different properties viz., metal spin state, redox potential etc., of the individual heme centers using ethane-bridged porphyrin dimer as a synthetic model of dihemes. The large differences in the structure and properties of the diheme complexes, as compared to the monoheme analogs, provide an unequivocal evidence of the role played by heme-heme interaction in the dihemes

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