Sulphur shuttling across a chaperone during molybdenum cofactor maturation

Pascal Arnoux (), Christian Ruppelt, Flore Oudouhou, Jérôme Lavergne, Marina I. Siponen, René Toci, Ralf R. Mendel, Florian Bittner, David Pignol, Axel Magalon and Anne Walburger ()
Additional contact information
Pascal Arnoux: Laboratoire de Bioénergétique Cellulaire, CEA, DSV, IBEB
Christian Ruppelt: Technical University
Flore Oudouhou: Aix Marseille Université, CNRS, IMM, LCB UMR 7283
Jérôme Lavergne: Laboratoire de Bioénergétique Cellulaire, CEA, DSV, IBEB
Marina I. Siponen: Laboratoire de Bioénergétique Cellulaire, CEA, DSV, IBEB
René Toci: Aix Marseille Université, CNRS, IMM, LCB UMR 7283
Ralf R. Mendel: Technical University
Florian Bittner: Technical University
David Pignol: Laboratoire de Bioénergétique Cellulaire, CEA, DSV, IBEB
Axel Magalon: Aix Marseille Université, CNRS, IMM, LCB UMR 7283
Anne Walburger: Aix Marseille Université, CNRS, IMM, LCB UMR 7283

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract Formate dehydrogenases (FDHs) are of interest as they are natural catalysts that sequester atmospheric CO2, generating reduced carbon compounds with possible uses as fuel. FDHs activity in Escherichia coli strictly requires the sulphurtransferase EcFdhD, which likely transfers sulphur from IscS to the molybdenum cofactor (Mo-bisPGD) of FDHs. Here we show that EcFdhD binds Mo-bisPGD in vivo and has submicromolar affinity for GDP—used as a surrogate of the molybdenum cofactor’s nucleotide moieties. The crystal structure of EcFdhD in complex with GDP shows two symmetrical binding sites located on the same face of the dimer. These binding sites are connected via a tunnel-like cavity to the opposite face of the dimer where two dynamic loops, each harbouring two functionally important cysteine residues, are present. On the basis of structure-guided mutagenesis, we propose a model for the sulphuration mechanism of Mo-bisPGD where the sulphur atom shuttles across the chaperone dimer.

Date: 2015
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DOI: 10.1038/ncomms7148

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