Cytochrome c' folding triggered by electron transfer: fast and slow formation of four-helix bundles.

ABSTRACT: Reduced (Fe(II)) Rhodopseudomonas palustris cytochrome c' (Cyt c') is more stable toward unfolding ([GuHCl](1/2) = 2.9(1) M) than the oxidized (Fe(III)) protein ([GuHCl](1/2) = 1.9(1) M). The difference in folding free energies (Delta Delta G(f) degrees = 70 meV) is less than half of the difference in reduction potentials of the folded protein (100 mV vs. NHE) and a free heme in aqueous solution ( approximately -150 mV). The spectroscopic features of unfolded Fe(II)-Cyt c' indicate a low-spin heme that is axially coordinated to methionine sulfur (Met-15 or Met-25). Time-resolved absorption measurements after CO photodissociation from unfolded Fe(II)(CO)-Cyt c' confirm that methionine can bind to the ferroheme on the microsecond time scale [k(obs) = 5(2) x 10(4) s(-1)]. Protein folding was

SUBMITTER: Lee JC 

PROVIDER: S-EPMC35415 | biostudies-literature | 2001 Jul

REPOSITORIES: biostudies-literature