Projects per year
Protein motions and enzyme catalysis are often linked. It is hypothesized that ultrafast vibrations (femtosecond-picosecond) enhance the rate of hydride transfer catalyzed by members of the Old Yellow Enzyme (OYE) family of ene-reductases. Here, we use time-resolved infrared spectroscopy in combination with stable ‘heavy’ isotopic labeling (2H, 13C, 15N) of protein and/or cofactor to probe the vibrational energy transfer (VET) between pentaerythritol tetranitrate reductase (a member of the OYE family), and its non-covalently bound flavin mononucleotide (FMN) cofactor. We show that when the FMN cofactor is photoexcited with visible light, vibrational energy is transferred from the flavin to the surrounding protein environment on the picosecond timescale. This finding expands the scope of VET investigation in proteins, which are limited by suitable intrinsic probes, and may have implications in the understanding of the mechanism of recently discovered photoactive flavoenzymes.
|Journal||The Journal of Physical Chemistry B|
|Early online date||4 Jun 2020|
|Publication status||E-pub ahead of print - 4 Jun 2020|
- time-resolved infrared
- heavy enzyme
- isotope effect
- isotopic labeling
- vibrational energy transfer
Research Beacons, Institutes and Platforms
- Manchester Institute of Biotechnology
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- 1 Finished
Heavy enzymes: Probing fast dynamics in enzyme catalysis by mass modulation
1/01/15 → 31/12/17