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Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-Resolved Infrared Spectroscopy

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Sommer,  Constanze
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Reijerse,  Eduard J.
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Birrell,  James A.
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Lubitz,  Wolfgang
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Sanchez, M. L. K., Sommer, C., Reijerse, E. J., Birrell, J. A., Lubitz, W., & Dyer, R. B. (2019). Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-Resolved Infrared Spectroscopy. The Journal of Organic Chemistry, 141(40), 16064-16070. doi:10.1021/jacs.9b08348.


Cite as: https://hdl.handle.net/21.11116/0000-0006-5DFA-9
Abstract
Hydrogenases are metalloenzymes that catalyze the reversible oxidation of H-2. The [FeFe] hydrogenases are generally biased toward proton reduction and have high activities. Several different catalytic mechanisms have been proposed for the [FeFe] enzymes based on the identification of intermediate states in equilibrium and steady state experiments. Here, we examine the kinetic competency of these intermediate states in the [FeFe] hydrogenase from Chlamydomonas reinhardtii (CrHydA1), using a laser-induced potential jump and time-resolved IR (TRIR) spectroscopy. A CdSe/CdS dot-in-rod (DIR) nanocrystalline semiconductor is employed as the photosensitizer and a redox mediator efficiently transfers electrons to the enzyme. A pulsed laser induces a potential jump, and TRIR spectroscopy is used to follow the population flux through each intermediate state. The results clearly establish the kinetic competency of all intermediate populations examined: H-ox, H-red, HredH+, HsredH+, and H-hyd. Additionally, a new short-lived intermediate species with a CO peak at 1896 cm(-1) was identified. These results establish a kinetics framework for understanding the catalytic mechanism of [FeFe] hydrogenases.