The interaction between horse cytochrome c and the tryptic fragment of bovine liver microsomal cytochrome b5 in the absence and presence of [Cr(ethylenediamine)3]Cl3 was studied by 1H NMR spectroscopy. The protein-protein interaction region on cytochrome b5 was found to be different from the [Cr(en)3]3+-binding region. The solvent-exposed propionate-bearing edge of the haem of cytochrome b5 is accessible to [Cr(en)3]3+ in the interprotein complex.
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Hartshorn et al. (1987) studied this question.
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