journal article·2025-10-16

Light-Powered Transport of Organic Anions by Microbial Rhodopsins

Simiao Shen, Shoichiro Akita, Joji Wada, Mako Eguchi, Takashi Tsukamoto, Kwang-Hwan Jung, Yuki Sudo, Takashi Kikukawa

Publisher page

Abstract

Microbial rhodopsins are photoactive membrane proteins known for transporting small inorganic ions such as H +, Cl –, and Na + . Their compact structure─comprising seven transmembrane helices─has long been thought to limit their substrate range to such ions. Here, we report that several anion-pumping rhodopsins can also transport organic anions. In particular, a rhodopsin from cyanobacteria transports bulky organic anions, including those with a benzene ring, with volumes up to ∼120 Å 3 ─five times larger than Cl – . These anions bind in the dark state and are translocated upon photoactivation, via a mechanism similar to Cl – . Notably, only anions with p K a values below 2 are transported, suggesting that negative charge is essential for binding. This study provides the first evidence that naturally occurring proteins can use light to transport organic compounds across membranes. These findings broaden the functional scope of microbial rhodopsins and open new possibilities for light-driven transport of organic ions.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Photoreceptor and optogenetics research · Molecular Communication and Nanonetworks · Neuroscience and Neuropharmacology Research

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Graduate School of Life Science

Hokkaido University

School of Science

Faculty of Advanced Life Science

Department of Life Science and Stress-Responding Bionanomaterial Center

Sogang University

Faculty of Medicine, Dentistry and Pharmaceutical Sciences

Okayama University

Funding

Steel Foundation for Environmental Protection Technology · Japan Society for the Promotion of Science · JKA Foundation · G-7 Scholarship Foundation

References (34)

Show source-provided references
1. 10.1021/cr400376910.1021/cr4003769 ↗
2. 10.1146/annurev-biochem-101910-14423310.1146/annurev-biochem-101910-144233 ↗
3. Gushchin I. · 2018 · 1910.1007/978-981-10-7757-9_2 ↗
4. 10.1007/s12551-020-00645-010.1007/s12551-020-00645-0 ↗
5. 10.1146/annurev-micro-031721-02045210.1146/annurev-micro-031721-020452 ↗
6. 10.1038/newbio233149a010.1038/newbio233149a0 ↗
7. 10.1073/pnas.70.10.285310.1073/pnas.70.10.2853 ↗
8. 10.1038/nn.409110.1038/nn.4091 ↗
9. 10.1039/D3CS00699A10.1039/D3CS00699A ↗
10. 10.1126/science.aan554410.1126/science.aan5544 ↗
11. 10.1126/science.aaa748410.1126/science.aaa7484 ↗
12. 10.1021/acs.biochem.9b0076810.1021/acs.biochem.9b00768 ↗
13. 10.1021/jacs.1c1260810.1021/jacs.1c12608 ↗
14. 10.1016/S0021-9258(19)40007-010.1016/S0021-9258(19)40007-0 ↗
15. 10.1529/biophysj.106.09315310.1529/biophysj.106.093153 ↗
16. 10.1021/jp507219q10.1021/jp507219q ↗
17. 10.1021/jacs.6b1213910.1021/jacs.6b12139 ↗
18. 10.1038/s41598-022-20784-610.1038/s41598-022-20784-6 ↗
19. 10.1126/science.abj666310.1126/science.abj6663 ↗
20. 10.1021/acs.jpcb.3c0211610.1021/acs.jpcb.3c02116 ↗
21. 10.1038/s41467-022-34019-910.1038/s41467-022-34019-9 ↗
22. 10.1038/nrm264610.1038/nrm2646 ↗
23. 10.1016/j.tibs.2013.01.00310.1016/j.tibs.2013.01.003 ↗
24. 10.1016/j.bbamem.2019.18315410.1016/j.bbamem.2019.183154 ↗
25. Kikukawa T. · 2021 · 5510.1007/978-981-15-8763-4_4 ↗
26. 10.1016/0006-291X(77)91245-110.1016/0006-291X(77)91245-1 ↗
27. 10.1016/S0021-9258(18)34020-110.1016/S0021-9258(18)34020-1 ↗
28. 10.1073/pnas.140305111110.1073/pnas.1403051111 ↗
29. 10.1074/jbc.M115.68861410.1074/jbc.M115.688614 ↗
30. 10.1021/bi00044a02710.1021/bi00044a027 ↗
31. 10.1002/cphc.20100018110.1002/cphc.201000181 ↗
32. 10.1002/anie.20210388210.1002/anie.202103882 ↗
33. 10.1016/j.jbc.2025.10833410.1016/j.jbc.2025.108334 ↗
34. 10.1021/jp803282s10.1021/jp803282s ↗