Characterization of the iron-sulfur protein of the mitochondrial outer membrane partially purified from beef kidney cortex
| Autor: | Anders Ehrenberg, Michele Lorusso, Dan Bäckström, Kristoffer Anderson |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Iron-Sulfur Proteins
inorganic chemicals Kidney Cortex Biophysics chemistry.chemical_element Mitochondrion Biochemistry law.invention Electron transfer law Oxidoreductase Metalloproteins Animals Inner membrane Electron paramagnetic resonance Cytochrome Reductases chemistry.chemical_classification Electron Spin Resonance Spectroscopy Membrane Proteins Cell Biology Sulfur Mitochondria Cortex (botany) Crystallography chemistry Spectrophotometry Cattle Bacterial outer membrane Oxidation-Reduction |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Bioenergetics. 502:276-288 |
| ISSN: | 0005-2728 |
| DOI: | 10.1016/0005-2728(78)90049-x |
| Popis: | The iron-sulfur protein present in the mitochondrial outer membrane has been partially purified from beef kidney cortex mitochondria be means of selective solubilization followed by DEAE-cellulose chromatography. The EPR spectrum of the iron-sulfur protein with g -values at 2.01, 1.94 and 1.89 was well resolved up to 200 K which is unusual for an iron-sulfur protein. Analyses confirmed a center with two iron and two labile sulfur atoms in the protein. By measuring the effect of oxidation-reduction potential on the EPR signal amplitude, midpoint potentials at pH 7.2 were determined both for the purified ironsulfur protein, +75 (±5) mV, and in prepared mitochondrial outer membrane, +62 (±6) mV. At pH 8.2 slightly lower values were indicated, +62 and 52 mV, respectively. The oxidation-reduction equilibrium involved a one electron transfer. A functional relationship to the rotenone-insensitive NADH-cytochrome c oxidoreductase in the mitochondrial outer membrane is suggested. Both this activity and the iron-sulfur center were sensitive to acidities slightly below pH 7 in contrast to the iron-sulfur centers of the inner membrane. |
| Databáze: | OpenAIRE |
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