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Understanding the Structure and Dynamics of Hydrogenases by Ultrafast and Two-Dimensional Infrared Spectroscopy

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Understanding the Structure and Dynamics of Hydrogenases by Ultrafast and Two-Dimensional Infrared Spectroscopy. / Hunt, Neil Terrence; Horch, Marius.

In: Chemical Science, 05.08.2019.

Research output: Contribution to journalArticlepeer-review

Harvard

Hunt, NT & Horch, M 2019, 'Understanding the Structure and Dynamics of Hydrogenases by Ultrafast and Two-Dimensional Infrared Spectroscopy', Chemical Science. https://doi.org/10.1039/C9SC02851J

APA

Hunt, N. T., & Horch, M. (2019). Understanding the Structure and Dynamics of Hydrogenases by Ultrafast and Two-Dimensional Infrared Spectroscopy. Chemical Science. https://doi.org/10.1039/C9SC02851J

Vancouver

Hunt NT, Horch M. Understanding the Structure and Dynamics of Hydrogenases by Ultrafast and Two-Dimensional Infrared Spectroscopy. Chemical Science. 2019 Aug 5. https://doi.org/10.1039/C9SC02851J

Author

Hunt, Neil Terrence ; Horch, Marius. / Understanding the Structure and Dynamics of Hydrogenases by Ultrafast and Two-Dimensional Infrared Spectroscopy. In: Chemical Science. 2019.

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@article{ce00bcce69ee441a91d34f3aef51527e,
title = "Understanding the Structure and Dynamics of Hydrogenases by Ultrafast and Two-Dimensional Infrared Spectroscopy",
abstract = "Hydrogenases are valuable model enzymes for sustainable energy conversion approaches using H2, but rational utilization of these base-metal biocatalysts requires a detailed understanding of the structure and dynamics of their complex active sites. The intrinsic CO and CN− ligands of these metalloenzymes represent ideal chromophores for infrared (IR) spectroscopy, but structural and dynamic insight from conventional IR absorption experiments is limited. Here, we apply ultrafast and two-dimensional (2D) IR spectroscopic techniques, for the first time, to study hydrogenases in detail. Using an O2-tolerant [NiFe] hydrogenase as a model system, we show that IR pump-probe spectroscopy can explore catalytically relevant ligand bonding by accessing high-lying vibrational states. This ultrafast technique also shows that the protein matrix is influential in vibrational relaxation, which may be relevant for energy dissipation from the active site during fast reaction steps. Further insights into the relevance of the active site environment are provided by 2D-IR spectroscopy, which reveals equilibrium dynamics and structural constraints imposed on the H2-accepting intermediate of [NiFe] hydrogenases. Both techniques offer new strategies for uniquely identifying redox-structural states in complex catalytic mixtures via vibrational quantum beats and 2D-IR off-diagonal peaks. Together, these findings considerably expand the scope of IR spectroscopy in hydrogenase research, and new perspectives for the characterization of these enzymes and other (bio‑)organometallic targets are presented.",
author = "Hunt, {Neil Terrence} and Marius Horch",
year = "2019",
month = aug,
day = "5",
doi = "10.1039/C9SC02851J",
language = "English",
journal = "Chemical Science",
issn = "2041-6520",
publisher = "The Royal Society of Chemistry",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Understanding the Structure and Dynamics of Hydrogenases by Ultrafast and Two-Dimensional Infrared Spectroscopy

AU - Hunt, Neil Terrence

AU - Horch, Marius

PY - 2019/8/5

Y1 - 2019/8/5

N2 - Hydrogenases are valuable model enzymes for sustainable energy conversion approaches using H2, but rational utilization of these base-metal biocatalysts requires a detailed understanding of the structure and dynamics of their complex active sites. The intrinsic CO and CN− ligands of these metalloenzymes represent ideal chromophores for infrared (IR) spectroscopy, but structural and dynamic insight from conventional IR absorption experiments is limited. Here, we apply ultrafast and two-dimensional (2D) IR spectroscopic techniques, for the first time, to study hydrogenases in detail. Using an O2-tolerant [NiFe] hydrogenase as a model system, we show that IR pump-probe spectroscopy can explore catalytically relevant ligand bonding by accessing high-lying vibrational states. This ultrafast technique also shows that the protein matrix is influential in vibrational relaxation, which may be relevant for energy dissipation from the active site during fast reaction steps. Further insights into the relevance of the active site environment are provided by 2D-IR spectroscopy, which reveals equilibrium dynamics and structural constraints imposed on the H2-accepting intermediate of [NiFe] hydrogenases. Both techniques offer new strategies for uniquely identifying redox-structural states in complex catalytic mixtures via vibrational quantum beats and 2D-IR off-diagonal peaks. Together, these findings considerably expand the scope of IR spectroscopy in hydrogenase research, and new perspectives for the characterization of these enzymes and other (bio‑)organometallic targets are presented.

AB - Hydrogenases are valuable model enzymes for sustainable energy conversion approaches using H2, but rational utilization of these base-metal biocatalysts requires a detailed understanding of the structure and dynamics of their complex active sites. The intrinsic CO and CN− ligands of these metalloenzymes represent ideal chromophores for infrared (IR) spectroscopy, but structural and dynamic insight from conventional IR absorption experiments is limited. Here, we apply ultrafast and two-dimensional (2D) IR spectroscopic techniques, for the first time, to study hydrogenases in detail. Using an O2-tolerant [NiFe] hydrogenase as a model system, we show that IR pump-probe spectroscopy can explore catalytically relevant ligand bonding by accessing high-lying vibrational states. This ultrafast technique also shows that the protein matrix is influential in vibrational relaxation, which may be relevant for energy dissipation from the active site during fast reaction steps. Further insights into the relevance of the active site environment are provided by 2D-IR spectroscopy, which reveals equilibrium dynamics and structural constraints imposed on the H2-accepting intermediate of [NiFe] hydrogenases. Both techniques offer new strategies for uniquely identifying redox-structural states in complex catalytic mixtures via vibrational quantum beats and 2D-IR off-diagonal peaks. Together, these findings considerably expand the scope of IR spectroscopy in hydrogenase research, and new perspectives for the characterization of these enzymes and other (bio‑)organometallic targets are presented.

U2 - 10.1039/C9SC02851J

DO - 10.1039/C9SC02851J

M3 - Article

JO - Chemical Science

JF - Chemical Science

SN - 2041-6520

ER -