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.
| Original language | English |
|---|---|
| Pages (from-to) | 3290-3293 |
| Number of pages | 4 |
| Journal | Journal of Physical Chemistry Letters |
| Volume | 7 |
| Issue number | 16 |
| DOIs | |
| Publication status | Published - Aug 18 2016 |
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ASJC Scopus subject areas
- Materials Science(all)
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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
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TY - JOUR
T1 - Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy
AU - Mirmohades, Mohammad
AU - Adamska-Venkatesh, Agnieszka
AU - Sommer, Constanze
AU - Reijerse, Edward
AU - Lomoth, Reiner
AU - Lubitz, Wolfgang
AU - Hammarström, Leif
PY - 2016/8/18
Y1 - 2016/8/18
N2 - 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.
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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U2 - 10.1021/acs.jpclett.6b01316
DO - 10.1021/acs.jpclett.6b01316
M3 - Article
AN - SCOPUS:84983261297
VL - 7
SP - 3290
EP - 3293
JO - Journal of Physical Chemistry Letters
JF - Journal of Physical Chemistry Letters
SN - 1948-7185
IS - 16
ER -