期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 14, 期 6, 页码 1485-1493出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpclett.2c03110
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In this study, the reaction dynamics of Chrimson channelrhodopsin were analyzed from femtoseconds to seconds. Multiple phases in the decay of excited state were identified, and early dynamics of K-like species on a 10 ps time scale were observed. Selective excitation at different wavelengths resulted in distinct spectral features, which gradually became indistinguishable over time. Protein motions underlying inhomogeneous broadening were resolved, demonstrating a dynamic interconversion between protein substates.
Chrimson is a red-light absorbing channelrhodopsin useful for deep-tissue optogenetics applications. Here, we present the Chrimson reaction dynamics from femtoseconds to seconds, analyzed with target analysis methods to disentangle spectrally and temporally overlapping excited-and product-state dynamics. We found multiple phases ranging from approximate to 100 fs to approximate to 20 ps in the excited-state decay, where spectral features overlapping with stimulated emission components were assigned to early dynamics of K-like species on a 10 ps time scale. Selective excitation at the maximum or the blue edge of the absorption spectrum resulted in spectrally distinct but kinetically similar excited-state and product-state species, which gradually became indistinguishable on the mu s to 100 mu s time scales. Hence, by removing specific protein conformations within an inhomoge-neously broadened ensemble, we resolved slow protein backbone and amino acid side-chain motions in the dark that underlie inhomogeneous broadening, demonstrating that the latter represents a dynamic interconversion between protein substates.
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