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Different chirality of the axial methionine in homologous cytochromes c determined by proton nmr and circular dichroism spectroscopy


, : Different chirality of the axial methionine in homologous cytochromes c determined by proton nmr and circular dichroism spectroscopy. Biochemical & Biophysical Research Communications 92(4): 1362-1369

The heme Fe coordination in horse cytochrome c and cytochrome c-551 from Pseudomonas aeruginosa was investigated with 1H NMR and CD [circular dichroism] spectroscopy. Truncated driven nuclear Overhauser enhancement (TOE) studies of the reduced proteins showed different chirality for the attachment of the axial methionine in the 2 spp. For the oxidized proteins the different chirality was manifested in different CD properties of the 695 nm adsorption band. Since additional NMR data indicated nearly identical coordination of the axial histidine in the 2 spp., the previously reported different electronic heme structures in the oxidized proteins may be a consequence of the different mode of binding of the axial methionine.

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