Photophosphorylation elements in halobacteria: an A-type ATP synthase and bacterial rhodopsins.
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.
Mukohata
Y
Y
Department of Biology, Faculty of Science, Nagoya University, Japan.
Sugiyama
Y
Y
Ihara
K
K
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000595:Amino Acid Sequence; D001436:Bacteriorhodopsins / Q000737:chemistry / Q000378:metabolism*; D006217:Halobacterium / Q000201:enzymology / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D010777:Photochemistry
D001436:Bacteriorhodopsins; D000251:Adenosine Triphosphatases