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

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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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Authors and Affiliations

  1. Department of Biology, Faculty of Science, Nagoya University, 464-01, Nagoya, Japan

    Yasuo Mukohata, Yasuo Sugiyama & Kunio Ihara

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  1. Yasuo Mukohata
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  2. Yasuo Sugiyama
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  3. Kunio Ihara
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Mukohata, Y., Sugiyama, Y. & Ihara, K. Photophosphorylation elements in halobacteria: An A-type ATP synthase and bacterial rhodopsins. J Bioenerg Biomembr 24, 547–553 (1992). https://doi.org/10.1007/BF00762347

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  • DOI: https://doi.org/10.1007/BF00762347

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