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Enhanced Oxygen-Tolerance of the Full Heterotrimeric Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha
[Image: see text] 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 t...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4073834/ https://www.ncbi.nlm.nih.gov/pubmed/24866391 http://dx.doi.org/10.1021/ja503138p |
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author | Radu, Valentin Frielingsdorf, Stefan Evans, Stephen D. Lenz, Oliver Jeuken, Lars J. C. |
author_facet | Radu, Valentin Frielingsdorf, Stefan Evans, Stephen D. Lenz, Oliver Jeuken, Lars J. C. |
author_sort | Radu, Valentin |
collection | PubMed |
description | [Image: see text] 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. |
format | Online Article Text |
id | pubmed-4073834 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-40738342014-07-07 Enhanced Oxygen-Tolerance of the Full Heterotrimeric Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha Radu, Valentin Frielingsdorf, Stefan Evans, Stephen D. Lenz, Oliver Jeuken, Lars J. C. J Am Chem Soc [Image: see text] 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. American Chemical Society 2014-05-27 2014-06-18 /pmc/articles/PMC4073834/ /pubmed/24866391 http://dx.doi.org/10.1021/ja503138p Text en Copyright © 2014 American Chemical Society Terms of Use CC-BY (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) |
spellingShingle | Radu, Valentin Frielingsdorf, Stefan Evans, Stephen D. Lenz, Oliver Jeuken, Lars J. C. Enhanced Oxygen-Tolerance of the Full Heterotrimeric Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha |
title | Enhanced
Oxygen-Tolerance of the Full Heterotrimeric
Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha |
title_full | Enhanced
Oxygen-Tolerance of the Full Heterotrimeric
Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha |
title_fullStr | Enhanced
Oxygen-Tolerance of the Full Heterotrimeric
Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha |
title_full_unstemmed | Enhanced
Oxygen-Tolerance of the Full Heterotrimeric
Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha |
title_short | Enhanced
Oxygen-Tolerance of the Full Heterotrimeric
Membrane-Bound [NiFe]-Hydrogenase of Ralstonia eutropha |
title_sort | enhanced
oxygen-tolerance of the full heterotrimeric
membrane-bound [nife]-hydrogenase of ralstonia eutropha |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4073834/ https://www.ncbi.nlm.nih.gov/pubmed/24866391 http://dx.doi.org/10.1021/ja503138p |
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