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  • Title: Interaction of cytochrome c with the blue copper proteins, plastocyanin and azurin.
    Author: Augustin MA, Chapman SK, Davies DM, Sykes AG, Speck SH, Margoliash E.
    Journal: J Biol Chem; 1983 May 25; 258(10):6405-9. PubMed ID: 6304038.
    Abstract:
    Bimolecular rate constants have been determined for the reactions of native horse cytochrome c, eight 4-carboxy-2,6-dinitrophenyl (CDNP-) cytochromes c singly modified at lysines 7, 13, 25, 27, 60, 72, 86, or 87 and one 2,3,6-trinitrophenyl cytochrome c singly modified at lysine 13, with the blue copper proteins, plastocyanin (from parsley leaves) and azurin (from Pseudomonas aeruginosa). Plastocyanin, a protein having a negative charge of about -7, yields a bimolecular rate constant with native ferrocytochrome c of 1.5 x 10(6) M-1 S-1, which decreases with the modified cytochromes c to a minimum of 7.5 x 10(5) M-1 S-1 for the CDNP-lysine 13 derivative. Conversely azurin, a protein with an overall negative charge of only about -1 to -2, exhibits bimolecular rate constants with native ferrocytochrome c of 6.6 x 10(3) M-1 S-1 at pH 6.1 and 4.0 x 10(3) M-1 S-1 at pH 8.6, which increase upon modification of the cytochrome c to a maximum of 4.1 x 10(4) M-1 S-1 at pH 6.1 and 2.7 x 10(4) M-1 S-1 at pH 8.6, for the CDNP-cytochrome c modified at lysine 72. This behavior indicates that: 1) the reaction of cytochrome c occurs at a negatively charged site on plastocyanin, whereas azurin behaves as a positively charged reactant, the electrostatics governing to a large extent the relative reactivities of the modified cytochromes c; 2) in both cases the interaction domain on cytochrome c is located on the "front" surface of the protein and encompasses the solvent accessible edge of the heme prosthetic group, as is the case for all the reactions of cytochrome c with its mitochondrial protein redox partners, as well as for small inorganic redox complexes; and 3) the bimolecular rate constants for plastocyanin and azurin are orders of magnitude slower and the effects of lysine modifications far smaller than for the reactions with physiological systems, indicating that: (a) the electric fields generated by the reactants do not align them, prior to electron transfer, as effectively as for the physiological reaction partners of cytochrome c; and (b) there is an absence of a precise molecular fit between cytochrome c and the nonphysiological redox partners.
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