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

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

doi:10.1021/acs.jpclett.6b01316

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

Mohammad Mirmohades, Agnieszka Adamska-Venkatesh, Constanze Sommer, Edward Reijerse, Reiner Lomoth, Wolfgang Lubitz, Leif Hammarström

Uppsala University

Research output: Contribution to journal › Article › peer-review

12 Citations (Scopus)

Abstract

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 ≈ 13 ± 5 ms at room temperature. This gives direct information on the dynamics of CO inhibition of the enzyme.

Original language	English
Pages (from-to)	3290-3293
Number of pages	4
Journal	Journal of Physical Chemistry Letters
Volume	7
Issue number	16
DOIs	https://doi.org/10.1021/acs.jpclett.6b01316
Publication status	Published - Aug 18 2016

ASJC Scopus subject areas

Materials Science(all)
Physical and Theoretical Chemistry

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Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy. / Mirmohades, Mohammad; Adamska-Venkatesh, Agnieszka; Sommer, Constanze; Reijerse, Edward; Lomoth, Reiner; Lubitz, Wolfgang; Hammarström, Leif.

In: Journal of Physical Chemistry Letters, Vol. 7, No. 16, 18.08.2016, p. 3290-3293.

Research output: Contribution to journal › Article › peer-review

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abstract = "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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AU - Mirmohades, Mohammad

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AU - Sommer, Constanze

AU - Reijerse, Edward

AU - Lomoth, Reiner

AU - Lubitz, Wolfgang

AU - Hammarström, Leif

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AB - 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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