AI Article Synopsis
- The discovery of rhodopsin 2 (KR2) in 2013 shifted the understanding of cation transport in microbial rhodopsins, now including sodium transport alongside protons.
- KR2's unique retinal binding pocket, featuring a strong interaction between the retinal Schiff base and counterion D116, is key to its photochemical behavior.
- The article reviews recent advancements in understanding KR2's functionality through photon absorption and highlights ongoing debates and future research directions in microbial rhodopsin photochemistry.
Article Abstract
The discovery of the light-driven sodium pump rhodopsin 2 (KR2) in 2013 has changed the paradigm that cation transport in microbial rhodopsins is restricted to the translocation of protons. Even though this finding is already remarkable by itself, it also reignited more general discussions about the functional mechanism of ion transport. The unique composition of the retinal binding pocket in KR2 with a tight interaction between the retinal Schiff base and its respective counterion D116 also has interesting implications on the photochemical pathway of the chromophore. Here, we discuss the most recent advances in our understanding of the KR2 functionality from the primary event of photon absorption by all- retinal up to the actual protein response in the later phases of the photocycle, mainly from the point of view of optical spectroscopy. In this context, we furthermore highlight some of the ongoing debates on the photochemistry of microbial rhodopsins and give some perspectives for promising future directions in this field of research.
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| http://dx.doi.org/10.1021/acs.jpcb.2c08933 | DOI Listing |
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Article Synopsis
- * The first discovered ion-pumping rhodopsin was bacteriorhodopsin in 1971, which pumps protons outward, and since then, various rhodopsins that transport protons, chloride, and sodium ions have been identified across different microorganisms.
- * Recent research focuses on understanding the conformational changes in inward and outward proton-pumping rhodopsins, utilizing time-resolved resonance Raman spectroscopy to explore their structures and mechanisms for unidirectional ion transport.
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