A spectroscopic method for observing the domain movement of the Rieske iron-sulfur protein.

ABSTRACT: The g-tensor orientation of the chemically reduced Rieske cluster in cytochrome bc(1) complex from Rhodovulum sulfidophilum with respect to the membrane was determined in the presence and absence of inhibitors and in the presence of oxidized and reduced quinone in the quinol-oxidizing-site (Q(o)-site) by EPR on two-dimensionally ordered samples. Almost identical orientations were observed when oxidized or reduced quinone, stigmatellin, or 5-(n-undecyl)-6-hydroxy-4,7-dioxobenzothiazole was present. Occupancy of the Q(o)-site by myxothiazole induced appearance of a minority population with a substantially differing conformation and presence of E-beta-methoxyacrylate-stilbene significantly reduced the contribution of the major conformation observed in the other cases. Furthermore, when the ox

SUBMITTER: Brugna M 

PROVIDER: S-EPMC15755 | biostudies-literature | 2000 Feb

REPOSITORIES: biostudies-literature