title: Following [FeFe] Hydrogenase Active Site Intermediates by Time-Resolved Mid-IR Spectroscopy.
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.
authors: Department of Chemistry - Ångström Laboratory, Uppsala University , Box 523, 751 20 Uppsala, Sweden.
authors: Mohammad
authors: M
authors: Mirmohades
authors: Max Planck Institute for Chemical Energy Conversion , Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
authors: Agnieszka
authors: A
authors: Adamska-Venkatesh
authors: Max Planck Institute for Chemical Energy Conversion , Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
authors: Constanze
authors: C
authors: Sommer
authors: Max Planck Institute for Chemical Energy Conversion , Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
authors: Edward
authors: E
authors: Reijerse
authors: Department of Chemistry - Ångström Laboratory, Uppsala University , Box 523, 751 20 Uppsala, Sweden.
authors: Reiner
authors: R
authors: Lomoth
authors: Max Planck Institute for Chemical Energy Conversion , Stiftstrasse 34-36, 45470 Mülheim an der Ruhr, Germany.
authors: Wolfgang
authors: W
authors: Lubitz
authors: Department of Chemistry - Ångström Laboratory, Uppsala University , Box 523, 751 20 Uppsala, Sweden.
authors: Leif
authors: L
authors: Hammarström