Ultrafast Vibrational Energy Transfer between Protein and Cofactor in a Flavoenzyme
| Autor: | Sam Hay, Derren J. Heyes, Andreea Iulia Iorgu, Samantha J. O. Hardman, Nigel S. Scrutton, Igor V. Sazanovich |
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| Rok vydání: | 2020 |
| Předmět: |
Flavin Mononucleotide
Flavin mononucleotide Flavin group 010402 general chemistry Photochemistry Vibration 01 natural sciences Article Catalysis Cofactor Enzyme catalysis Isotopic labeling chemistry.chemical_compound Manchester Institute of Biotechnology Flavins 0103 physical sciences Kinetic isotope effect Materials Chemistry Physical and Theoretical Chemistry Spectroscopy isotopic labeling 010304 chemical physics biology Chemistry Hydride ResearchInstitutes_Networks_Beacons/manchester_institute_of_biotechnology heavy enzyme 0104 chemical sciences Surfaces Coatings and Films Energy Transfer biology.protein time-resolved infrared vibrational energy transfer isotope effect |
| Zdroj: | The Journal of Physical Chemistry. B Hardman, S J O, Iorgu, A I, Heyes, D J, Scrutton, N S, Sazanovich, I V & Hay, S 2020, ' Ultrafast Vibrational Energy Transfer between Protein and Cofactor in a Flavoenzyme ', The Journal of Physical Chemistry B . https://doi.org/10.1021/acs.jpcb.0c04929 |
| ISSN: | 1520-5207 1520-6106 |
| DOI: | 10.1021/acs.jpcb.0c04929 |
| Popis: | 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 (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 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. |
| Databáze: | OpenAIRE |
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