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001052090 0247_ $$2doi$$a10.1021/acs.jpcb.4c08416
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001052090 1001_ $$00009-0006-6743-2344$$aLamm, Gerrit H. U.$$b0
001052090 245__ $$aCombined Mutational and Spectroscopic Study on the Calcium-Related Kinetic Effects on the VirChR1 Photocycle
001052090 260__ $$aWashington, DC$$bAmerical Chemical Society$$c2025
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001052090 520__ $$aThe viral rhodopsin 1 subfamily consists of microbial rhodopsins, such as VirChR1, with a light-gated cation channeling functionality, which is inhibited by calcium. For VirChR1, S14, E54, and N225 have been proposed as key residues for calcium binding. They form a highly conserved SEN-triad in channelrhodopsins near the functionally important central gate. Here, we present a time-resolved UV/vis spectroscopic study on the VirChR1 variants S14A, E54A, and N225A in a calcium-dependent manner. Comparison with the calcium-associated effects observed for the wild type shed light on the role of the respective residues for the calcium interaction. While S14A shows less pronounced, yet similar, signals, indicative of a reduced calcium affinity, E54A exhibits nearly calcium-independent photocycle kinetics, highlighting its crucial role for calcium binding. The N225A variant shows altered photocycle kinetics, in both the absence and presence of calcium, demonstrating its critical role in the formation of the functionally important central gate in VirChR1.
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001052090 7001_ $$0P:(DE-Juel1)176570$$aZabelskii, Dmitrii$$b1
001052090 7001_ $$0P:(DE-Juel1)131949$$aBalandin, Taras$$b2
001052090 7001_ $$0P:(DE-Juel1)131964$$aGordeliy, Valentin$$b3
001052090 7001_ $$00000-0002-8496-8240$$aWachtveitl, Josef$$b4$$eCorresponding author
001052090 773__ $$0PERI:(DE-600)2006039-7$$a10.1021/acs.jpcb.4c08416$$gVol. 129, no. 11, p. 2946 - 2957$$n11$$p2946 - 2957$$tThe journal of physical chemistry / B$$v129$$x1520-6106$$y2025
001052090 8564_ $$uhttps://juser.fz-juelich.de/record/1052090/files/combined-mutational-and-spectroscopic-study-on-the-calcium-related-kinetic-effects-on-the-virchr1-photocycle.pdf$$yOpenAccess
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