Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.

Formaldehyde-a rapid and reversible inhibitor of hydrogen evolution by [FeFe]-hydrogenases-binds with a strong potential dependence that is almost complementary to that of CO. Whereas exogenous CO binds tightly to the oxidized state known as H(ox) but very weakly to a state two electrons more reduce...

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Main Authors: Foster, C, Krämer, T, Wait, A, Parkin, A, Jennings, D, Happe, T, McGrady, J, Armstrong, F
Format: Journal article
Language:English
Published: 2012
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author Foster, C
Krämer, T
Wait, A
Parkin, A
Jennings, D
Happe, T
McGrady, J
Armstrong, F
author_facet Foster, C
Krämer, T
Wait, A
Parkin, A
Jennings, D
Happe, T
McGrady, J
Armstrong, F
author_sort Foster, C
collection OXFORD
description Formaldehyde-a rapid and reversible inhibitor of hydrogen evolution by [FeFe]-hydrogenases-binds with a strong potential dependence that is almost complementary to that of CO. Whereas exogenous CO binds tightly to the oxidized state known as H(ox) but very weakly to a state two electrons more reduced, formaldehyde interacts most strongly with the latter. Formaldehyde thus intercepts increasingly reduced states of the catalytic cycle, and density functional theory calculations support the proposal that it reacts with the H-cluster directly, most likely targeting an otherwise elusive and highly reactive Fe-hydrido (Fe-H) intermediate.
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spelling oxford-uuid:72c7fd66-16c6-4260-857b-0dbe67becedb2022-03-26T19:52:17ZInhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:72c7fd66-16c6-4260-857b-0dbe67becedbEnglishSymplectic Elements at Oxford2012Foster, CKrämer, TWait, AParkin, AJennings, DHappe, TMcGrady, JArmstrong, FFormaldehyde-a rapid and reversible inhibitor of hydrogen evolution by [FeFe]-hydrogenases-binds with a strong potential dependence that is almost complementary to that of CO. Whereas exogenous CO binds tightly to the oxidized state known as H(ox) but very weakly to a state two electrons more reduced, formaldehyde interacts most strongly with the latter. Formaldehyde thus intercepts increasingly reduced states of the catalytic cycle, and density functional theory calculations support the proposal that it reacts with the H-cluster directly, most likely targeting an otherwise elusive and highly reactive Fe-hydrido (Fe-H) intermediate.
spellingShingle Foster, C
Krämer, T
Wait, A
Parkin, A
Jennings, D
Happe, T
McGrady, J
Armstrong, F
Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.
title Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.
title_full Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.
title_fullStr Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.
title_full_unstemmed Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.
title_short Inhibition of [FeFe]-hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation.
title_sort inhibition of fefe hydrogenases by formaldehyde and wider mechanistic implications for biohydrogen activation
work_keys_str_mv AT fosterc inhibitionoffefehydrogenasesbyformaldehydeandwidermechanisticimplicationsforbiohydrogenactivation
AT kramert inhibitionoffefehydrogenasesbyformaldehydeandwidermechanisticimplicationsforbiohydrogenactivation
AT waita inhibitionoffefehydrogenasesbyformaldehydeandwidermechanisticimplicationsforbiohydrogenactivation
AT parkina inhibitionoffefehydrogenasesbyformaldehydeandwidermechanisticimplicationsforbiohydrogenactivation
AT jenningsd inhibitionoffefehydrogenasesbyformaldehydeandwidermechanisticimplicationsforbiohydrogenactivation
AT happet inhibitionoffefehydrogenasesbyformaldehydeandwidermechanisticimplicationsforbiohydrogenactivation
AT mcgradyj inhibitionoffefehydrogenasesbyformaldehydeandwidermechanisticimplicationsforbiohydrogenactivation
AT armstrongf inhibitionoffefehydrogenasesbyformaldehydeandwidermechanisticimplicationsforbiohydrogenactivation