Tuning of B photochemistry in the CarH photoreceptor to avoid radical photoproducts. | LitMetric

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Tuning of B photochemistry in the CarH photoreceptor to avoid radical photoproducts. | LitMetric

Tuning of B photochemistry in the CarH photoreceptor to avoid radical photoproducts.

Ines S Camacho Emma Wall Igor V Sazanovich Emma Gozzard Mike Towrie Neil T Hunt Sam Hay Alex R Jones

Chem Commun (Camb)

Biometrology, Chemical and Biological Sciences Department, National Physical Laboratory, Teddington, Middlesex, UK.

Published: October 2023

Time-resolved infrared spectroscopy is used to study how electron density moves through coenzyme B in the light-activated protein CarH.
CarH serves as a bacterial transcriptional regulator that stabilizes charge transfer states.
This stabilization helps manage the photoresponse, preventing the formation of harmful radical photoproducts.

Time-resolved infrared spectroscopy reveals the flow of electron density through coenzyme B in the light-activated, bacterial transcriptional regulator, CarH. The protein stabilises a series of charge transfer states that result in a photoresponse that avoids reactive, and potentially damaging, radical photoproducts.

Download full-text PDF	Source
http://dx.doi.org/10.1039/d3cc03900e	DOI Listing

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