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Stimulation of ATP synthesis in Halobacterium halobium R1 by light-induced or artifically created proton electrochemical potential gradients across the cell membrane.

The relationship between proton movement and phosphorylation in Halo-bacterium halobium R1 has been investigated under anaerobic conditions. The light-induced changes in the bacteriorhodopsin are accompanied by proton movements across the membrane which result in pH changes in the suspending medium. The initial alkaline shift is shown to be closely paralleled by (and hence correlated with) ATP synthesis. Acidification of the medium in the presence of valinomycin, under conditions of low external potassium, brings about ATP synthesis in the dark.

Adenosine Triphosphate↗

Effect of light-adaptation on the photoreaction of bacteriorhodopsin from Halobacterium halobium.

Light-induced formation of the 410 nm intermediate was investigated on dark-and light-adapted bacteriorhodopsin. The amplitude of the light-induced absorption increase at 410 nm of the light-adapted bacteriorhodopsin was twice as large as that of the dark-adapted bacteriorhodopsin. The amount of protons released from bacteriorhodopsin in response to illumination was also enhanced by light-adaptation. The degree of the enhancement was independent of the temperature in the dark-adaptation. The relation between these photochemical events and the isomeric configurations of retinal is discussed.

Adaptation, Physiological↗

Ion effects on protein-nucleic acid interactions: the disassembly of the 50-S ribosomal subunit from the halophilic bacterium, Halobacterium cutirubrum.

The 50-S ribosomal subunits from the extreme halophilic bacterium, Halo-bacterium cutirubrum, stable structurally and functionally in concentrated salt solutions were subjected to ionic environments depleted in either K+ or Mg2+ or both. Under these conditions specific classes of proteins are released from the subunit along with the 5 S RNA. Two-dimensional electrophoretic analysis of the resultant split protein fractions indicate some mutually exclusive effects of specific ions on the binding of specific proteins to the 23 S RNA as well as on the retention of 5 S RNA within the ribosomal macrostructure.

Bacterial Proteins↗