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Review
. 1992 Dec;24(6):547-53.
doi: 10.1007/BF00762347.

Photophosphorylation elements in halobacteria: an A-type ATP synthase and bacterial rhodopsins

Y Mukohata  1 , Y Sugiyama, K Ihara
Affiliations
Review

Photophosphorylation elements in halobacteria: an A-type ATP synthase and bacterial rhodopsins

Y Mukohata et al. J Bioenerg Biomembr. 1992 Dec.

Abstract

Photophosphorylation in halobacteria is carried out by two rather simple elements: an A-type ATP synthase and light-driven ion-pumping bacterial rhodopsins. The unique features of halobacterial ATP synthase, mostly common to archaebacteria (A-type), and of new members of the bacteriorhodopsin family are introduced along with studies performed in the authors' laboratory. This is the story of how we found that the A-type ATP synthase is close to V-type ATPase but far from F-type ATPase, although all three ATPases are believed to have the same ancestor. Archaerhodopsins, the new members of the proton-pumping retinal proteins, were found in Australian halobacteria and have been used in a comparative study of bacterial rhodopsins.

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