Sensors 2009, 9(12), 9741-9804; doi:10.3390/s91209741

Photoreactions and Structural Changes of Anabaena Sensory Rhodopsin

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Received: 18 September 2009; in revised form: 14 October 2009 / Accepted: 23 October 2009 / Published: 3 December 2009
(This article belongs to the Special Issue Microbial Sensors and Biosensors)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract: Anabaena sensory rhodopsin (ASR) is an archaeal-type rhodopsin found in eubacteria. The gene encoding ASR forms a single operon with ASRT (ASR transducer) which is a 14 kDa soluble protein, suggesting that ASR functions as a photochromic sensor by activating the soluble transducer. This article reviews the detailed photoreaction processes of ASR, which were studied by low-temperature Fourier-transform infrared (FTIR) and UV-visible spectroscopy. The former research reveals that the retinal isomerization is similar to bacteriorhodopsin (BR), but the hydrogen-bonding network around the Schiff base and cytoplasmic region is different. The latter study shows the stable photoproduct of the all-trans form is 100% 13-cis, and that of the 13-cis form is 100% all-trans. These results suggest that the structural changes of ASR in the cytoplasmic domain play important roles in the activation of the transducer protein, and photochromic reaction is optimized for its sensor function.
Keywords: photosensor; rhodopsin; photochromism; FTIR spectroscopy; UV-visible spectroscopy
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MDPI and ACS Style

Kawanabe, A.; Kandori, H. Photoreactions and Structural Changes of Anabaena Sensory Rhodopsin. Sensors 2009, 9, 9741-9804.

AMA Style

Kawanabe A, Kandori H. Photoreactions and Structural Changes of Anabaena Sensory Rhodopsin. Sensors. 2009; 9(12):9741-9804.

Chicago/Turabian Style

Kawanabe, Akira; Kandori, Hideki. 2009. "Photoreactions and Structural Changes of Anabaena Sensory Rhodopsin." Sensors 9, no. 12: 9741-9804.

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