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The adrenodoxin-like ferredoxin of Schizosaccharomyces pombe mitochondria

Item Type:Article
Title:The adrenodoxin-like ferredoxin of Schizosaccharomyces pombe mitochondria
Creators Name:Schiffler, B. and Bureik, M. and Reinle, W. and Mueller, E.C. and Hannemann, F. and Bernhardt, R.
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 11β (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.
Keywords:Electron-Transfer-Protein 1, Etp1 Fd, Functional Dimer, Mitochondrial Ferredoxin, Schizosaccharomyces Pombe, Animals, Cattle
Source:Journal of Inorganic Biochemistry
Page Range:1229-1237
Date:1 January 2004
Official Publication:https://doi.org/10.1016/j.jinorgbio.2004.02.006
PubMed:View item in PubMed

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