REVIEW] An Inward Proton Transport Using Anabaena Sensory Rhodopsin

Akira Kawanabe; Yuji Furutani; Kwang-Hwan Jung; Hideki Kandori

doi:10.1007/s12275-011-0547-x

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REVIEW] An Inward Proton Transport Using Anabaena Sensory Rhodopsin: Akira Kawanabe ^1,2, Yuji Furutani ^1,3, Kwang-Hwan Jung ⁴, Hideki Kandori ¹; Journal of Microbiology 2011;49(1):1-6.
DOI: https://doi.org/10.1007/s12275-011-0547-x
Published online: March 3, 2011

¹Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan, ²Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka 565-0871, Japan, ³Department of Life and Coordination-Complex Molecular Science, Institute for Molecular Science, 38 Nishigo-Naka, Myodaiji, Okazaki 444-8585, Japan, ⁴Department of Life Science and Institute of Biological Interfaces, Sogang University, Seoul 121-742, Republic of Korea¹Department of Frontier Materials, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan, ²Graduate School of Medicine, Osaka University, Yamadaoka 2-2, Suita, Osaka 565-0871, Japan, ³Department of Life and Coordination-Complex Molecular Science, Institute for Molecular Science, 38 Nishigo-Naka, Myodaiji, Okazaki 444-8585, Japan, ⁴Department of Life Science and Institute of Biological Interfaces, Sogang University, Seoul 121-742, Republic of Korea

Corresponding author: Hideki Kandori , Tel: +81-52-735-5027,

Received: 31 December 2010 • Accepted: 14 January 2011

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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.

Keywords: microbial rhodopsin;photochromism;proton pump;retinal;FTIR

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REVIEW] An Inward Proton Transport Using Anabaena Sensory Rhodopsin

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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