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TitlePhototrophy by antenna-containing rhodopsin pumps in aquatic environments.
Journal, issue, pagesNature, Vol. 615, Issue 7952, Page 535-540, Year 2023
Publish dateMar 1, 2023
AuthorsAriel Chazan / Ishita Das / Takayoshi Fujiwara / Shunya Murakoshi / Andrey Rozenberg / Ana Molina-Márquez / Fumiya K Sano / Tatsuki Tanaka / Patricia Gómez-Villegas / Shirley Larom / Alina Pushkarev / Partha Malakar / Masumi Hasegawa / Yuya Tsukamoto / Tomohiro Ishizuka / Masae Konno / Takashi Nagata / Yosuke Mizuno / Kota Katayama / Rei Abe-Yoshizumi / Sanford Ruhman / Keiichi Inoue / Hideki Kandori / Rosa León / Wataru Shihoya / Susumu Yoshizawa / Mordechai Sheves / Osamu Nureki / Oded Béjà /
PubMed AbstractEnergy transfer from light-harvesting ketocarotenoids to the light-driven proton pump xanthorhodopsins has been previously demonstrated in two unique cases: an extreme halophilic bacterium and a ...Energy transfer from light-harvesting ketocarotenoids to the light-driven proton pump xanthorhodopsins has been previously demonstrated in two unique cases: an extreme halophilic bacterium and a terrestrial cyanobacterium. Attempts to find carotenoids that bind and transfer energy to abundant rhodopsin proton pumps from marine photoheterotrophs have thus far failed. Here we detected light energy transfer from the widespread hydroxylated carotenoids zeaxanthin and lutein to the retinal moiety of xanthorhodopsins and proteorhodopsins using functional metagenomics combined with chromophore extraction from the environment. The light-harvesting carotenoids transfer up to 42% of the harvested energy in the violet- or blue-light range to the green-light absorbing retinal chromophore. Our data suggest that these antennas may have a substantial effect on rhodopsin phototrophy in the world's lakes, seas and oceans. However, the functional implications of our findings are yet to be discovered.
External linksNature / PubMed:36859551
MethodsEM (single particle) / X-ray diffraction
Resolution2.3 - 3 Å
Structure data

35143

8i2z

EMDB-35143, PDB-8i2z:
Cryo-EM structure of the zeaxanthin-bound kin4B8
Method: EM (single particle) / Resolution: 2.3 Å

PDB-7ytb:
Crystal structure of Kin4B8
Method: X-RAY DIFFRACTION / Resolution: 3.0 Å

Chemicals

ChemComp-RET:
RETINAL

ChemComp-OLC:
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

ChemComp-HOH:
WATER

ChemComp-K3I:
Zeaxanthin

Source
  • uncultured bdellovibrionales bacterium (environmental samples)
  • bdellovibrio (bacteria)
KeywordsMEMBRANE PROTEIN / rhodopsin / inward proton pump / PROTON TRANSPORT / Cryo-EM / anntena

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