Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of ralstonia eutropha.
Radu, V, Frielingsdorf, S, Evans, SD et al. (2 more authors)
(2014)
Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of ralstonia eutropha.
Journal of the American Chemical Society, 136 (24).
8512 - 8515.
ISSN 0002-7863
Abstract
Hydrogenases are oxygen-sensitive enzymes that catalyze the conversion between protons and hydrogen. Water-soluble subcomplexes of membrane-bound [NiFe]-hydrogenases (MBH) have been extensively studied for applications in hydrogen-oxygen fuel cells as they are relatively tolerant to oxygen, although even these catalysts are still inactivated in oxidative conditions. Here, the full heterotrimeric MBH of Ralstonia eutropha, including the membrane-integral cytochrome b subunit, was investigated electrochemically using electrodes modified with planar tethered bilayer lipid membranes (tBLM). Cyclic voltammetry and chronoamperometry experiments show that MBH, in equilibrium with the quinone pool in the tBLM, does not anaerobically inactivate under oxidative redox conditions. In aerobic environments, the MBH is reversibly inactivated by O2, but reactivation was found to be fast even under oxidative redox conditions. This enhanced resistance to inactivation is ascribed to the oligomeric state of MBH in the lipid membrane.
Metadata
Authors/Creators:
Radu, V
Frielingsdorf, S
Evans, SD
Lenz, O
Jeuken, LJ
Copyright, Publisher and Additional Information:
(c) 2014, Radu, V, Frielingsdorf, S, Evans, SD, Lenz, O and Jeuken, LJ. This is an Open Access article distributed in accordance with the Creative Commons Attribution (CC BY 4.0) licence, which permits others to distribute, remix, adapt, build upon this work, and license their derivative works on different terms, provided the original work is properly cited.
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