Adjacent cysteines are capable of ligating the same tetranuclear iron-sulfur cluster

Proteins
Marion Gurrath, Thorsten Friedrich

Abstract

The mechanism of the energy-converting NADH (beta-nicotinamide adenine dinucleotide, reduced form):ubiquinone oxidoreductase, which is also called respiratory complex I, is largely unknown due to lack of a high-resolution structure and the most complicated construction of the enzyme. Electron transport is carried out by one flavin mononucleotide (FMN) and up to 9 Fe/S clusters. The Fe/S cluster N2, which is believed to be directly involved in redox-coupled proton-translocation, is located on subunit NuoB (the homologue of the mitochondrial PSST subunit). This subunit contains a conserved binding motif for a [4Fe/4S] cluster with two adjacent cysteines. It was questioned whether these adjacent cysteines could be ligands of the same cluster due to a possible steric hinderance. However, mutagenesis of either of these cysteines led to a loss of cluster N2. We used the known structure of the homologous small subunit of hydrogenases containing a regular cysteine motif to generate an in silico mutant with two consecutive cysteines. Molecular dynamics simulation showed that the conformation of these cysteines does not meet the topological requirements for coordination of a [4Fe/4S] cluster when the protein backbone conformation is kept...Continue Reading

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Citations

Jun 8, 2006·Annual Review of Biochemistry·Ulrich Brandt
Apr 29, 2006·Journal of Molecular Microbiology and Biotechnology·Dirk FlemmingThorsten Friedrich
Jul 13, 2005·PLoS Biology·Kate S CarrollCarolyn R Bertozzi
Jul 16, 2014·Journal of Bioenergetics and Biomembranes·Thorsten Friedrich
Apr 16, 2009·Biochimica Et Biophysica Acta·Volker ZickermannUlrich Brandt
May 25, 2010·Biochimica Et Biophysica Acta·Maja A TocilescuUlrich Brandt
Apr 1, 2007·EcoSal Plus·Thorsten Friedrich, Thomas Pohl

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