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Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Mirmohades, Mohammad Adamska-Venkatesh, Agnieszka Sommer, Constanze Reijerse, Edward J. Lomoth, Reiner Lubitz, Wolfgang Hammarström, Leif |
| Copyright Year | 2016 |
| 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. |
| File Format | PDF HTM / HTML |
| DOI | 10.1021/acs.jpclett.6b01316 |
| PubMed reference number | 27494400 |
| Journal | Medline |
| Volume Number | 7 |
| Issue Number | 16 |
| Alternate Webpage(s) | http://uu.diva-portal.org/smash/get/diva2:970726/FULLTEXT01.pdf |
| Alternate Webpage(s) | https://doi.org/10.1021/acs.jpclett.6b01316 |
| Journal | The journal of physical chemistry letters |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |
