The cytochrome c' from Chromatium vinosum has been studied through 'H NMR in the pH range 4-l 1 in both the oxidized and the reduced forms. The iH NMR spectra are similar to those of the other cytochrome c' systems. Three pK, values of 5.1, 7.0, and 9.2 have been observed for the oxidized species and tentatively assigned to the two carboxylate propionic residues of the heme moiety and to the iron-coordinated histidine 125, respectively. The spectra are consistent with an essentially S = Fj state in all the pH ranges investigated. Some evidence is provided for conformational flexibilities. Among the oxidized cytochromes c' the present one is capable of binding cyanide, giving rise to a low spin state. The reduced species is a typical high spin iron (II) system.
H NMR Studies of Chromatium vinosum Cytochrome c´
1990
Abstract
The cytochrome c' from Chromatium vinosum has been studied through 'H NMR in the pH range 4-l 1 in both the oxidized and the reduced forms. The iH NMR spectra are similar to those of the other cytochrome c' systems. Three pK, values of 5.1, 7.0, and 9.2 have been observed for the oxidized species and tentatively assigned to the two carboxylate propionic residues of the heme moiety and to the iron-coordinated histidine 125, respectively. The spectra are consistent with an essentially S = Fj state in all the pH ranges investigated. Some evidence is provided for conformational flexibilities. Among the oxidized cytochromes c' the present one is capable of binding cyanide, giving rise to a low spin state. The reduced species is a typical high spin iron (II) system.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
