Ultrafast Vibrational Energy Transfer between Protein and Cofactor in a Flavoenzyme
Open Access
- 25 June 2020
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 124 (25), 5163-5168
- https://doi.org/10.1021/acs.jpcb.0c04929
Abstract
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 (TRIR) spectroscopy in combination with stable "heavy" isotopic labeling (H-2, C-13, N-15) of protein and/or cofactor to probe the vibrational energy transfer (VET) between pentaerythritol tetranitrate reductase (a member of the OYE family) and its noncovalently 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.Funding Information
- Biotechnology and Biological Sciences Research Council (BB/M007065/1, BB/S003320/1)
This publication has 35 references indexed in Scilit:
- Proteins in Action: Femtosecond to Millisecond Structural Dynamics of a Photoactive FlavoproteinJournal of the American Chemical Society, 2013
- Fast Protein Motions Are Coupled to Enzyme H-Transfer ReactionsJournal of the American Chemical Society, 2013
- Vibrational Assignment of the Ultrafast Infrared Spectrum of the Photoactivatable Flavoprotein AppAThe Journal of Physical Chemistry B, 2012
- Ultrafast Infrared Spectroscopy of an Isotope-Labeled Photoactivatable FlavoproteinBiochemistry, 2011
- Biocatalytic Reductions and Chemical Versatility of the Old Yellow Enzyme Family of Flavoprotein OxidoreductasesChemCatChem, 2010
- Can infrared spectroscopy provide information on protein–protein interactions?Biochemical Society Transactions, 2010
- Evidence To Support the Hypothesis That Promoting Vibrations Enhance the Rate of an Enzyme Catalyzed H-Tunneling ReactionJournal of the American Chemical Society, 2009
- Infrared spectroscopy of proteinsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2007
- Ultrafast Vibrational Spectroscopy of the Flavin ChromophoreThe Journal of Physical Chemistry B, 2006
- Potential of carbon-13 and nitrogen-15 labeling for studying protein-protein interactions using Fourier-transform infrared spectroscopyBiochemistry, 1992