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- Reisomerization Preceding Reprotonation of the Retinal Chromophore Is Common to the Schizorhodopsin Family: A Simple and Rational Mechanism for Inward Proton Pumping.
J Phys Chem B
January 2024
Department of Chemistry, Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka 560-0043, Japan.
The creation of unidirectional ion transporters across membranes represents one of the greatest challenges in chemistry. Proton-pumping rhodopsins are composed of seven transmembrane helices with a retinal chromophore bound to a lysine side chain via a Schiff base linkage and provide valuable insights for designing such transporters. What makes these transporters particularly intriguing is the discovery of both outward and inward proton-pumping rhodopsins.
View Article and Find Full Text PDFComparative Genomic Analyses of the Genus Unravels the Genomic Adaptation to Polar Extreme Environments.
Microorganisms
January 2022
State Key Laboratory of Lake Science and Environment, Nanjing Institute of Geography and Limnology, Chinese Academy of Sciences, 73 East Beijing Road, Nanjing 210008, China.
The members of the genus have been isolated from various habitats, like saline soil, salt lake, sponge-associated and the human gut, some of which are even located in polar areas. To identify their stress resistance mechanisms and draw a genomic profile across this genus, we isolated four strains from the lakes in the Tibetan Plateau, referred to as the third pole, and compared them with all other 30 high-quality genomes that are deposited in NCBI. The Heaps' law model estimated that the pan-genome of this genus is open and the number of core, shell, cloud, and singleton genes were 993 (6.
View Article and Find Full Text PDFPhotochemistry of Bacteriorhodopsin with Various Oligomeric Statuses in Controlled Membrane Mimicking Environments: A Spectroscopic Study from Femtoseconds to Milliseconds.
J Phys Chem B
March 2019
Department of Chemistry , National Tsing Hua University, 101, Sec. 2, Kuang-Fu Road , Hsinchu 30013 , Taiwan.
Preparing transmembrane protein in controllable lipid bilayers is essential for unravelling the coupling of the environments and its dynamic functions. Monomerized bacteriorhodopsin (mbR) embedded in covalently circularized nanodiscs was prepared with dimyristoylphosphatidylglycerol (DMPG) lipid and circular membrane scaffold proteins of two different sizes, cE3D1 and cΔ H5, respectively. The retinal photoisomerization kinetics and thermodynamic photocycle were examined by femtosecond and nanosecond transient absorption, respectively, covering the time scale from femtoseconds to hundreds of milliseconds.
View Article and Find Full Text PDFUnraveling the mechanism of proton translocation in the extracellular half-channel of bacteriorhodopsin.
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May 2016
Physics Department, City College of New York, New York, NY, 10031.
Bacteriorhodopsin, a light activated protein that creates a proton gradient in halobacteria, has long served as a simple model of proton pumps. Within bacteriorhodopsin, several key sites undergo protonation changes during the photocycle, moving protons from the higher pH cytoplasm to the lower pH extracellular side. The mechanism underlying the long-range proton translocation between the central (the retinal Schiff base SB216, D85, and D212) and exit clusters (E194 and E204) remains elusive.
View Article and Find Full Text PDFPhotochemistry of a dual-bacteriorhodopsin system in Haloarcula marismortui: HmbRI and HmbRII.
J Phys Chem B
July 2014
Department of Chemistry, National Tsing Hua University, 101, Sec. 2, Kuang-Fu Road, Hsinchu 30013, Taiwan.
Recently, a dual-bacteriorhodopsin system, containing HmbRI and HmbRII, has been found in Haloarcula marismortui (Mol. Microbiol. 2013, 88, 551-561), and the light-driven proton pump activities were intrinsically different in a wide pH range.
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