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Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Physical Chemistry.
Max Planck Inst Chem Energy Convers, Stiftstr 34-36, D-45470 Mulheim, Germany..
Max Planck Inst Chem Energy Convers, Stiftstr 34-36, D-45470 Mulheim, Germany..
Max Planck Inst Chem Energy Convers, Stiftstr 34-36, D-45470 Mulheim, Germany..
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2016 (English)In: Journal of Physical Chemistry Letters, ISSN 1948-7185, E-ISSN 1948-7185, Vol. 7, no 16, 3290-3293 p.Article in journal (Refereed) Published
Abstract [en]

Time-resolved nanosecond mid-infrared spectroscopy is for the first time employed to study the [FeFe] hydrogenase from Chlamydomonas reinhardtii and to investigate relevant intermediates of the enzyme active site. An actinic 355 nm, 10 ns laser flash triggered photodissociation of a carbonyl group from the CO-inhibited state H-ox-CO to form the state H-ox, which is an intermediate of the catalytic proton reduction cycle. Time-resolved infrared spectroscopy allowed us to directly follow the subsequent rebinding of the carbonyl, re-forming H-ox-CO, and determine the reaction half-life to be t(1/2) approximate to 13 +/- 5 ms at room temperature. This gives direct information GO on the dynamics of CO inhibition of the enzyme.

Place, publisher, year, edition, pages
2016. Vol. 7, no 16, 3290-3293 p.
National Category
Physical Chemistry
URN: urn:nbn:se:uu:diva-303048DOI: 10.1021/acs.jpclett.6b01316ISI: 000381781800036PubMedID: 27494400OAI: oai:DiVA.org:uu-303048DiVA: diva2:970726
Knut and Alice Wallenberg FoundationSwedish Energy AgencySwedish Research CouncilMax Planck Society
Available from: 2016-09-14 Created: 2016-09-14 Last updated: 2016-09-14Bibliographically approved

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