title: The adrenodoxin-like ferredoxin of Schizosaccharomyces pombe mitochondria.
abstract: The single mitochondrial type I [2Fe-2S] ferredoxin of the fission yeast Schizosaccharomyces pombe is produced as the carboxy terminal part of the electron-transfer-protein 1 (etp1) and cleaved off during mitochondrial import [Biochemistry 41 (2002) 2311-2321]. The UV/Vis (UV-visible) spectrum of the purified recombinant ferredoxin domain (etp1(fd)) expressed in Escherichia coli is similar to those of bovine Adx in the oxidized as well as in the reduced state. EPR (electronic paramagnetic resonance) studies revealed a correctly incorporated iron-sulfur cluster of the axial type. The redox potential of this protein was determined to be -353 mV, which is considerably lower than that of adrenodoxin (Adx, -273 mV). Several lines of evidence indicate that the protein forms dimers under physiological and denaturating conditions. Interestingly, the fission yeast ferredoxin could be shown to be active as an electron carrier in heterologous redox systems. It is able to transfer electrons to horse heart cytochrome c and to bovine cytochromes P450(scc) (CYP11A1) and P450(11 beta) (CYP11B1), thereby receiving electrons from bovine NADPH-dependent Adx reductase. The kinetics of substrate conversion in the etp1(fd)-supported CYP11A1 and CYP11B1-dependent systems mediated was studied.
authors.affiliation: Naturwissenschaftlich-Technische Fakultät III, FR 8.8-Biochemie, Universität des Saarlandes, P.O. Box 151150, D-66041 Saarbruecken, Germany.
authors.forename: Burkhard
authors.initials: B
authors.lastname: Schiffler
authors.forename: Matthias
authors.initials: M
authors.lastname: Bureik
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Reinle
authors.forename: Eva-Christina
authors.initials: EC
authors.lastname: Müller
authors.forename: Frank
authors.initials: F
authors.lastname: Hannemann
authors.forename: Rita
authors.initials: R
authors.lastname: Bernhardt
mesh_terms: D000325:Adrenodoxin; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002786:Cholesterol Side-Chain Cleavage Enzyme / Q000737:chemistry; D005288:Ferredoxins / Q000737:chemistry* / Q000235:genetics; D008928:Mitochondria / Q000201:enzymology*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012568:Schizosaccharomyces / Q000201:enzymology* / Q000235:genetics; D029702:Schizosaccharomyces pombe Proteins / Q000737:chemistry* / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013252:Steroid 11-beta-Hydroxylase / Q000737:chemistry
chemical_list: C081714:2Fe-2S ferredoxin; D005288:Ferredoxins; D011994:Recombinant Proteins; D029702:Schizosaccharomyces pombe Proteins; D000325:Adrenodoxin; D013252:Steroid 11-beta-Hydroxylase; D002786:Cholesterol Side-Chain Cleavage Enzyme