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

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


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 languageEnglish
Pages (from-to)3290-3293
Number of pages4
JournalJournal of Physical Chemistry Letters
Issue number16
Publication statusPublished - Aug 18 2016

ASJC Scopus subject areas

  • Materials Science(all)
  • Physical and Theoretical Chemistry

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