Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 7, Issue 16, Pages 3290-3293Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.6b01316
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- Knut and Alice Wallenberg Foundation
- Swedish Energy Agency
- Swedish Research Council
- Max Planck Society
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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.
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