title: Redox components of cytochrome bc-type enzymes in acidophilic prokaryotes. I. Characterization of the cytochrome bc1-type complex of the acidophilic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans.
abstract: The redox components of the cytochrome bc1 complex from the acidophilic chemolithotrophic organism Thiobacillus ferrooxidans were investigated by potentiometric and spectroscopic techniques. Optical redox titrations demonstrated the presence of two b-type hemes with differing redox midpoint potentials at pH 7.4 (-169 and + 20 mV for bL and bH, respectively). At pH 3.5, by contrast, both hemes appeared to titrate at about +20 mV. Antimycin A, 2-heptyl-4-hydroxyquinoline N-oxide, and stigmatellin induced distinguishable shifts of the b hemes' alpha-bands, providing evidence for the binding of antimycin A and 2-heptyl-4-hydroxyquinoline N-oxide near heme bH (located on the cytosolic side of the membrane) and of stigmatellin near heme bL (located on the periplasmic side of the membrane). The inhibitors stigmatellin, 5-(n-undecyl)-6-hydroxy-4,7-dioxobenzothiazole, and 2, 5-dibromo-3-methyl-6-isopropyl-p-benzoquinone affected the EPR spectrum of the Rieske iron-sulfur center in a way that differs from what has been observed for cytochrome bc1 or b6f complexes. The results obtained demonstrate that the T. ferrooxidans complex, although showing most of the features characteristic for bc1 complexes, contains unique properties that are most probably related to the chemolithotrophicity and/or acidophilicity of its parent organism. A speculative model for reverse electron transfer through the T. ferrooxidans complex is proposed.
authors.affiliation: Laboratoire de Bioénergétique et Ingéniérie des Proteines, CNRS, Institut de Biologie Structurale et Microbiologie, 31 chemin Joseph Aiguier, 13402 Marseille Cedex 20, France.
authors.forename: A
authors.initials: A
authors.lastname: Elbehti
authors.forename: W
authors.initials: W
authors.lastname: Nitschke
authors.forename: P
authors.initials: P
authors.lastname: Tron
authors.forename: C
authors.initials: C
authors.lastname: Michel
authors.forename: D
authors.initials: D
authors.lastname: Lemesle-Meunier
mesh_terms: D000968:Antimycin A / Q000494:pharmacology; D004578:Electron Spin Resonance Spectroscopy; D014450:Electron Transport Complex III / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D005296:Ferrous Compounds / Q000378:metabolism; D006418:Heme / Q000031:analogs & derivatives / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D006912:Hydroxyquinolines / Q000494:pharmacology; D007501:Iron / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism; D008689:Methacrylates; D008956:Models, Chemical; D010084:Oxidation-Reduction; D011090:Polyenes / Q000494:pharmacology; D011199:Potentiometry; D018892:Proton-Motive Force / Q000187:drug effects; D013045:Species Specificity; D013053:Spectrophotometry; D013816:Thermodynamics; D013844:Thiazoles / Q000494:pharmacology; D013855:Thiobacillus / Q000201:enzymology*
chemical_list: D005296:Ferrous Compounds; D006912:Hydroxyquinolines; D007506:Iron-Sulfur Proteins; D008689:Methacrylates; D011090:Polyenes; C037989:Rieske iron-sulfur protein; D013844:Thiazoles; C001333:2-(n-heptyl)-4-hydroxyquinoline N-oxide; C031690:heme C; D006418:Heme; D000968:Antimycin A; C030517:myxothiazol; C041573:stigmatellin; D007501:Iron; D014450:Electron Transport Complex III