Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment

Neil Terrence Hunt; Alison Parkin; Jason Martin Lynam; Anthony William Parker; Gregory M Greetham; Jamie Blaza; Yvonne Rippers; Julia Walton; Michael Towrie; Emily Saxton; Marius Horch; Barbara Procacci; Solomon Wrathall; Chris Furlan

doi:10.1039/d2cp04188j

Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment

Neil Terrence Hunt, Alison Parkin, Jason Martin Lynam, Anthony William Parker, Gregory M Greetham, Jamie Blaza, Yvonne Rippers, Julia Walton, Michael Towrie, Emily Saxton, Marius Horch, Barbara Procacci, Solomon Wrathall, Chris Furlan

Chemistry

Research output: Contribution to journal › Article › peer-review

Original language	English
Number of pages	17
Journal	Physical Chemistry Chemical Physics
Early online date	30 Sept 2022
DOIs	https://doi.org/10.1039/d2cp04188j
Publication status	E-pub ahead of print - 30 Sept 2022

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10.1039/d2cp04188jLicence: CC BY

EcHyd1_2D-IR main text RevisedAccepted author manuscript, 2.21 MB
Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment
© the Owner Societies 2022
Final published version, 2.89 MBLicence: CC BY

Fourier Transform Bioelectrochemistry
Parkin, A. (Keynote/plenary speaker)
22 Aug 2024
Activity: Talk or presentation › Invited talk
New methods for enzyme voltammetry
Parkin, A. (Invited speaker)
15 Sept 2022
Activity: Talk or presentation › Invited talk

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Hunt, N. T., Parkin, A., Lynam, J. M., Parker, A. W., Greetham, G. M., Blaza, J., Rippers, Y., Walton, J., Towrie, M., Saxton, E., Horch, M., Procacci, B., Wrathall, S., & Furlan, C. (2022). Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment. Physical Chemistry Chemical Physics. Advance online publication. https://doi.org/10.1039/d2cp04188j

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title = "Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment",

author = "Hunt, {Neil Terrence} and Alison Parkin and Lynam, {Jason Martin} and Parker, {Anthony William} and Greetham, {Gregory M} and Jamie Blaza and Yvonne Rippers and Julia Walton and Michael Towrie and Emily Saxton and Marius Horch and Barbara Procacci and Solomon Wrathall and Chris Furlan",

note = "{\textcopyright} the Owner Societies 2022",

year = "2022",

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doi = "10.1039/d2cp04188j",

language = "English",

journal = "Physical Chemistry Chemical Physics",

issn = "1463-9076",

publisher = "The Royal Society of Chemistry",

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Hunt, NT , Parkin, A , Lynam, JM, Parker, AW, Greetham, GM, Blaza, J, Rippers, Y, Walton, J, Towrie, M, Saxton, E, Horch, M , Procacci, B, Wrathall, S & Furlan, C 2022, 'Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment', Physical Chemistry Chemical Physics. https://doi.org/10.1039/d2cp04188j

TY - JOUR

T1 - Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment

AU - Hunt, Neil Terrence

AU - Parkin, Alison

AU - Lynam, Jason Martin

AU - Parker, Anthony William

AU - Greetham, Gregory M

AU - Blaza, Jamie

AU - Rippers, Yvonne

AU - Walton, Julia

AU - Towrie, Michael

AU - Saxton, Emily

AU - Horch, Marius

AU - Procacci, Barbara

AU - Wrathall, Solomon

AU - Furlan, Chris

PY - 2022/9/30

Y1 - 2022/9/30

U2 - 10.1039/d2cp04188j

DO - 10.1039/d2cp04188j

M3 - Article

SN - 1463-9076

JO - Physical Chemistry Chemical Physics

JF - Physical Chemistry Chemical Physics

ER -

Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment

Bibliographical note

Access to Document

Activities

Fourier Transform Bioelectrochemistry

New methods for enzyme voltammetry

Cite this