Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases.
The extraordinary ability of Fe- and Ni-containing enzymes to catalyze rapid and efficient H(+)/H(2) interconversion--a property otherwise exclusive to platinum metals--has been investigated in a series of experiments combining variable-temperature protein film voltammetry with mathematical modeling...
Huvudupphovsmän: | , , , , |
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Materialtyp: | Journal article |
Språk: | English |
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2012
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_version_ | 1826292285685366784 |
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author | Hexter, S Grey, F Happe, T Climent, V Armstrong, F |
author_facet | Hexter, S Grey, F Happe, T Climent, V Armstrong, F |
author_sort | Hexter, S |
collection | OXFORD |
description | The extraordinary ability of Fe- and Ni-containing enzymes to catalyze rapid and efficient H(+)/H(2) interconversion--a property otherwise exclusive to platinum metals--has been investigated in a series of experiments combining variable-temperature protein film voltammetry with mathematical modeling. The results highlight important differences between the catalytic performance of [FeFe]-hydrogenases and [NiFe]-hydrogenases and justify a simple model for reversible catalytic electron flow in enzymes and electrocatalysts that should be widely applicable in fields as diverse as electrochemistry, catalysis, and bioenergetics. The active site of [FeFe]-hydrogenases, an intricate Fe-carbonyl complex known as the "H cluster," emerges as a supreme catalyst. |
first_indexed | 2024-03-07T03:12:20Z |
format | Journal article |
id | oxford-uuid:b49e12c7-b99e-4e37-aeef-715a0798c29c |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-07T03:12:20Z |
publishDate | 2012 |
record_format | dspace |
spelling | oxford-uuid:b49e12c7-b99e-4e37-aeef-715a0798c29c2022-03-27T04:27:26ZElectrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b49e12c7-b99e-4e37-aeef-715a0798c29cEnglishSymplectic Elements at Oxford2012Hexter, SGrey, FHappe, TCliment, VArmstrong, FThe extraordinary ability of Fe- and Ni-containing enzymes to catalyze rapid and efficient H(+)/H(2) interconversion--a property otherwise exclusive to platinum metals--has been investigated in a series of experiments combining variable-temperature protein film voltammetry with mathematical modeling. The results highlight important differences between the catalytic performance of [FeFe]-hydrogenases and [NiFe]-hydrogenases and justify a simple model for reversible catalytic electron flow in enzymes and electrocatalysts that should be widely applicable in fields as diverse as electrochemistry, catalysis, and bioenergetics. The active site of [FeFe]-hydrogenases, an intricate Fe-carbonyl complex known as the "H cluster," emerges as a supreme catalyst. |
spellingShingle | Hexter, S Grey, F Happe, T Climent, V Armstrong, F Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. |
title | Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. |
title_full | Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. |
title_fullStr | Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. |
title_full_unstemmed | Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. |
title_short | Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. |
title_sort | electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases |
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