Cluster N1 of complex I from Yarrowia lipolytica studied by pulsed EPR spectroscopy

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
T MalyThomas F Prisner

Abstract

After reduction with nicotinamide adenine dinucleotide (NADH), NADH:ubiquinone oxidoreductase (complex I) of the strictly aerobic yeast Yarrowia lipolytica shows clear signals from five different paramagnetic iron-sulfur (FeS) clusters (N1-N5) which can be detected using electron paramagnetic resonance (EPR) spectroscopy. The ligand environment and the assignment of several FeS clusters to specific binding motifs found in several subunits of the complex are still under debate. In order to characterize the hyperfine interaction of the surrounding nuclei with FeS cluster N1, one- and two-dimensional electron spin echo envelope modulation experiments were performed at a temperature of 30 K. At this temperature only cluster N1 contributes to the overall signal in a pulsed EPR experiment. The hyperfine and quadrupole tensors of a nitrogen nucleus and the isotropic and dipolar hyperfine couplings of two sets of protons could be determined by numerical simulation of the one- and two-dimensional spectra. The values obtained are in perfect agreement with a ferredoxin-like binding structure by four cysteine amino acid residues and allow the assignment of the nitrogen couplings to a backbone nitrogen nucleus and the proton couplings to th...Continue Reading

References

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Citations

Apr 16, 2009·Biochimica Et Biophysica Acta·Thorsten MalyThomas F Prisner
May 29, 2016·Journal of Inorganic Biochemistry·John J WrightMaxie M Roessler
Apr 26, 2012·Critical Reviews in Food Science and Nutrition·Fabiola MárquezJ Salas-Salvadó
Jun 13, 2019·Nature Communications·Marius SchulteThorsten Friedrich
Oct 22, 2009·Accounts of Chemical Research·Sevdalina LyubenovaThomas Prisner

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