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 |
ASJC Scopus subject areas
- Materials Science(all)
- Physical and Theoretical Chemistry
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Mirmohades, M., Adamska-Venkatesh, A., Sommer, C., Reijerse, E., Lomoth, R., Lubitz, W., & Hammarström, L. (2016). Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy. Journal of Physical Chemistry Letters, 7(16), 3290-3293. https://doi.org/10.1021/acs.jpclett.6b01316