期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 136, 期 24, 页码 8512-8515出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja503138p
关键词
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资金
- European Research Council under the European Union [280518]
- DFG cluster of Excellence Unifying Concepts in Catalysis
- European Research Council (ERC) [280518] Funding Source: European Research Council (ERC)
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 O-2, 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.
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