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- REVIEW] An Inward Proton Transport Using Anabaena Sensory Rhodopsin
- Akira Kawanabe , Yuji Furutani , Kwang-Hwan Jung , Hideki Kandori
- J. Microbiol. 2011;49(1):1-6. Published online March 3, 2011
- DOI: https://doi.org/10.1007/s12275-011-0547-x
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- 8 Crossref
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Abstract
- ATP is synthesized by an enzyme that utilizes proton motive force and thus nature creates various proton pumps. The best understood proton pump is bacteriorhodopsin (BR), an outward-directed light-driven proton pump in Halobacterium salinarum. Many archaeal and eubacterial rhodopsins are now known to show similar proton transport activity. Proton pumps must have a specific mechanism to exclude transport in the reverse direction to maintain a proton gradient, and in the case of BR, a highly hydrophobic cytoplasmic domain may constitute such machinery. Although an inward proton pump has neither been created naturally nor artificially, we recently reported that an inward-directed proton transport can be engineered from a bacterial rhodopsin by a single amino acid replacement. Anabaena sensory rhodopsin (ASR) is a photochromic sensor in freshwater cyanobacteria, possessing little proton transport activity. When we replace Asp217 at the cytoplasmic domain (distance ~15 Å from the retinal chromophore) to Glu, ASR is converted into an inward proton transport, driven by absorption of a single photon. FTIR spectra clearly show an increased proton affinity for Glu217, which presumably controls the unusual directionality opposite to normal proton pumps.
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Citations
Citations to this article as recorded by
- Ion-transporting mechanism in microbial rhodopsins: Mini-review relating to the session 5 at the 19th International Conference on Retinal Proteins
Yuji Furutani, Chii-Shen Yang
Biophysics and Physicobiology.2023; 20(Supplement): n/a. CrossRef - Bioinformatic analysis of the distribution of inorganic carbon transporters and prospective targets for bioengineering to increase Ci uptake by cyanobacteria
Sandeep B. Gaudana, Jan Zarzycki, Vamsi K. Moparthi, Cheryl A. Kerfeld
Photosynthesis Research.2015; 126(1): 99. CrossRef - Chimeric Proton-Pumping Rhodopsins Containing the Cytoplasmic Loop of Bovine Rhodopsin
Kengo Sasaki, Takahiro Yamashita, Kazuho Yoshida, Keiichi Inoue, Yoshinori Shichida, Hideki Kandori, Karl-Wilhelm Koch
PLoS ONE.2014; 9(3): e91323. CrossRef - A role of Anabaena sensory rhodopsin transducer (ASRT) in photosensory transduction
So Young Kim, Sa Ryong Yoon, SongI Han, Yuna Yun, Kwang‐Hwan Jung
Molecular Microbiology.2014; 93(3): 403. CrossRef - The role of protein-bound water molecules in microbial rhodopsins
Klaus Gerwert, Erik Freier, Steffen Wolf
Biochimica et Biophysica Acta (BBA) - Bioenergetics.2014; 1837(5): 606. CrossRef - Microcompartments and Protein Machines in Prokaryotes
Milton H. Saier Jr.
Microbial Physiology.2013; 23(4-5): 243. CrossRef - Quantum chemical modeling of rhodopsin mutants displaying switchable colors
Federico Melaccio, Nicolas Ferré, Massimo Olivucci
Physical Chemistry Chemical Physics.2012; 14(36): 12485. CrossRef - Crystal Structure of the Eukaryotic Light-Driven Proton-Pumping Rhodopsin, Acetabularia Rhodopsin II, from Marine Alga
Takashi Wada, Kazumi Shimono, Takashi Kikukawa, Masakatsu Hato, Naoko Shinya, So Young Kim, Tomomi Kimura-Someya, Mikako Shirouzu, Jun Tamogami, Seiji Miyauchi, Kwang-Hwan Jung, Naoki Kamo, Shigeyuki Yokoyama
Journal of Molecular Biology.2011; 411(5): 986. CrossRef
- Ion-transporting mechanism in microbial rhodopsins: Mini-review relating to the session 5 at the 19th International Conference on Retinal Proteins
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