Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy | Zendy

Mohammad Mirmohades | Zendy; Agnieszka Adamska-Venkatesh | Zendy; Constanze Sommer | Zendy; Edward J. Reijerse | Zendy; Reiner Lomoth | Zendy; Wolfgang Lubitz | Zendy; Leif Hammarström | Zendy

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Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy

Author(s) -

Mohammad Mirmohades,

Agnieszka Adamska-Venkatesh,

Constanze Sommer,

Edward J. Reijerse,

Reiner Lomoth,

Wolfgang Lubitz,

Leif Hammarström

Publication year - 2016

Publication title -

the journal of physical chemistry letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.563

H-Index - 203

ISSN - 1948-7185

DOI - 10.1021/acs.jpclett.6b01316

Subject(s) - hydrogenase , photochemistry , active site , chemistry , hox gene , spectroscopy , photodissociation , chlamydomonas reinhardtii , infrared spectroscopy , nanosecond , catalysis , catalytic cycle , laser , physics , organic chemistry , biochemistry , quantum mechanics , transcription factor , mutant , optics , gene

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 Hox-CO to form the state Hox, 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 Hox-CO, and determine the reaction half-life to be t1/2 ≈ 13 ± 5 ms at room temperature. This gives direct information on the dynamics of CO inhibition of the enzyme.

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