Author
Listed:
- Keiichi Inoue
(Nagoya Institute of Technology
OptoBioTechnology Research Center, Nagoya Institute of Technology
PRESTO, Japan Science and Technology Agency)
- Shota Ito
(Nagoya Institute of Technology)
- Yoshitaka Kato
(Nagoya Institute of Technology)
- Yurika Nomura
(Nagoya Institute of Technology)
- Mikihiro Shibata
(Kanazawa University
Bio-AFM Frontier Research Center, Kanazawa University)
- Takayuki Uchihashi
(Kanazawa University
Bio-AFM Frontier Research Center, Kanazawa University)
- Satoshi P. Tsunoda
(Nagoya Institute of Technology)
- Hideki Kandori
(Nagoya Institute of Technology
OptoBioTechnology Research Center, Nagoya Institute of Technology)
Abstract
Light-driven outward H+ pumps are widely distributed in nature, converting sunlight energy into proton motive force. Here we report the characterization of an oppositely directed H+ pump with a similar architecture to outward pumps. A deep-ocean marine bacterium, Parvularcula oceani, contains three rhodopsins, one of which functions as a light-driven inward H+ pump when expressed in Escherichia coli and mouse neural cells. Detailed mechanistic analyses of the purified proteins reveal that small differences in the interactions established at the active centre determine the direction of primary H+ transfer. Outward H+ pumps establish strong electrostatic interactions between the primary H+ donor and the extracellular acceptor. In the inward H+ pump these electrostatic interactions are weaker, inducing a more relaxed chromophore structure that leads to the long-distance transfer of H+ to the cytoplasmic side. These results demonstrate an elaborate molecular design to control the direction of H+ transfers in proteins.
Suggested Citation
Keiichi Inoue & Shota Ito & Yoshitaka Kato & Yurika Nomura & Mikihiro Shibata & Takayuki Uchihashi & Satoshi P. Tsunoda & Hideki Kandori, 2016.
"A natural light-driven inward proton pump,"
Nature Communications, Nature, vol. 7(1), pages 1-10, December.
Handle:
RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms13415
DOI: 10.1038/ncomms13415
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