Bacterial rhodopsin: evidence for a new type of phototrophy in the sea.

@article{Bj2000BacterialRE,
  title={Bacterial rhodopsin: evidence for a new type of phototrophy in the sea.},
  author={Oded B{\'e}j{\`a} and L. Aravind and Eugene V. Koonin and M. T. Suzuki and Andrew G. Hadd and L P Nguyen and Stevan B. Jovanovich and Chris Gates and Robert Alan Feldman and John L. Spudich and Elena N. Spudich and Edward F. Delong},
  journal={Science},
  year={2000},
  volume={289 5486},
  pages={
          1902-6
        }
}
Extremely halophilic archaea contain retinal-binding integral membrane proteins called bacteriorhodopsins that function as light-driven proton pumps. So far, bacteriorhodopsins capable of generating a chemiosmotic membrane potential in response to light have been demonstrated only in halophilic archaea. We describe here a type of rhodopsin derived from bacteria that was discovered through genomic analyses of naturally occuring marine bacterioplankton. The bacterial rhodopsin was encoded in the… 
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References

SHOWING 1-10 OF 43 REFERENCES
A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-like photochemically reactive pigment.
TLDR
Laser flash kinetic spectroscopy demonstrates that the retinal-reconstituted pigment undergoes a photochemical reaction cycle with a near-UV-absorbing intermediate that is similar to the M intermediates produced by transient Schiff base deprotonation of the chromophore in the photocycles of bacteriorhodopsin and sensory rhodopsins I and II.
Molecular mechanism of photosignaling by archaeal sensory rhodopsins.
TLDR
The SR-Htr signaling complexes allow studies of the biophysical chemistry of signal generation and relay, from the photobiophysics of initial excitation of the receptors to the final output at the level of the flagellar motor switch, revealing fundamental principles of sensory transduction.
Primary structure of an archaebacterial transducer, a methyl-accepting protein associated with sensory rhodopsin I.
  • V. J. Yao, J. Spudich
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1992
TLDR
The results extend the eubacterial transducer family to the archaebacteria and substantiate the proposal that the methylated membrane protein functions as a signal-transducing relay between sensory rhodopsin I and cytoplasmic sensory-pathway components.
Evidence for massive gene exchange between archaeal and bacterial hyperthermophiles.
Understanding structure and function in the light-driven proton pump bacteriorhodopsin.
  • J. Lanyi
  • Biology, Chemistry
    Journal of structural biology
  • 1998
TLDR
The atomic structure of bacteriorhodopsin and the outlines of its proton transport mechanism are now available and the directionality of the translocation is ensured by the accessibility of the Schiff base to the extracellular and cytoplasmic directions after the retinal is photoisomerized.
Rhodopsin-like protein from the purple membrane of Halobacterium halobium.
TLDR
It is shown that the purple colour is due to retinal bound to an opsin-like protein, the only protein present in this membrane fragment, which has been isolated in relatively pure form from Halobacterium halobium.
The transducer protein HtrII modulates the lifetimes of sensory rhodopsin II photointermediates.
Structure of bacteriorhodopsin at 1.55 A resolution.
TLDR
The results indicate extensive involvement of bound water molecules in both the structure and the function of this seven-helical membrane protein.
Proton transfer reactions across bacteriorhodopsin and along the membrane.
  • J. Heberle
  • Biology, Chemistry
    Biochimica et biophysica acta
  • 2000
Biochemical analysis of spontaneous fepA mutants of Escherichia coli.
TLDR
The variation in endpoints among the deletions argues against the involvement of a normal transposon in their formation and unexpected homology was found between enterobactin gene cluster DNA and lacPOZ and pSC101.
...
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