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Reversible [4Fe-3S] cluster morphing in an O2-tolerant [NiFe] hydrogenase
Citation key ISI:000334672700012
Author Frielingsdorf, Stefan and Fritsch, Johannes and Schmidt, Andrea and Hammer, Mathias and Loewenstein, Julia and Siebert, Elisabeth and Pelmenschikov, Vladimir and Jaenicke, Tina and Kalms, Jacqueline and Rippers, Yvonne and Lendzian, Friedhelm and Zebger, Ingo and Teutloff, Christian and Kaupp, Martin and Bittl, Robert and Hildebrandt, Peter and Friedrich, Baerbel and Lenz, Oliver and Scheerer, Patrick
Pages 378-U92
Year 2014
ISSN 1552-4450
DOI 10.1038/nchembio.1500
Address 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA
Journal NATURE CHEMICAL BIOLOGY
Volume 10
Number 5
Month MAY
Publisher NATURE PUBLISHING GROUP
Abstract Hydrogenases catalyze the reversible oxidation of H-2 into protons and electrons and are usually readily inactivated by O-2. However, a subgroup of the [NiFe] hydrogenases, including the membrane-bound [NiFe] hydrogenase from Ralstonia eutropha, has evolved remarkable tolerance toward O-2 that enables their host organisms to utilize H-2 as an energy source at high O-2. This feature is crucially based on a unique six cysteine-coordinated [4Fe-3S] cluster located close to the catalytic center, whose properties were investigated in this study using a multidisciplinary approach. The [4Fe-3S] cluster undergoes redox-dependent reversible transformations, namely iron swapping between a sulfide and a peptide amide N. Moreover, our investigations unraveled the redox-dependent and reversible occurence of an oxygen ligand located at a different iron. This ligand is hydrogen bonded to a conserved histidine that is essential for H-2 oxidation at high O-2. We propose that these transformations, reminiscent of those of the P-cluster of nitrogenase, enable the consecutive transfer of two electrons within a physiological potential range.
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