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![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Proton coupled electron transfer in myoglobin compound II auto-reduction revealed by temperature dependent rate
Meghan B Mouton1, Olivia Browne1, Breanna G Bailey1
1Department of Chemistry, Xavier University of Louisiana, 1 Drexel Dr., New Orleans, LA 70125, USA.
None:
Myoglobin Compound II auto-reduction has been hypothesized to be sequential proton transfer followed by an electron transfer rate-limited via the protonation of the ferryl oxo with a pKa ≤ 2.7 via various spectroscopic techniques or 4.7 via UV-Visible spectroscopy and kinetic studies. However, by exploring the subtle pH and temperature dependence of kobs, we have found the Compound II auto-reduction to be best modeled with a pre-equilibrium proton transfer that includes both the sequential proton electron transfer and concerted proton-coupled electron transfer, gated by the distal Histidine64 as a proton donor. Parameters from the temperature dependence studies allow an extension of the proposed proton-coupled electron transfer model to fit the kobs to over full temperature range of 20⎼50 °C.
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