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At least 577 records · Page 32Linked to original sources
PubMed1980

Light-driven primary sodium ion transport in Halobacterium halobium membranes.

Light-induced sodium extrusion from H halobium cell envelope vesicles proceeds largely through an uncoupler-sensitive pathway involving bacteriorhodopsin and a proton/sodium antiporter. Vesicles from bacteriorhodopsin-negative strains also extrude sodium ions during illumination, but this transport is not sensitive to uncouplers and has been proposed to involve a light-energized primary sodium pump. Proton uptake in such vesicles is passive, and under steady-state illumination the large electrical potential (negative inside) is just balanced by a pH difference (acid inside), so that the proton-motive force is near zero. Action spectra indicated that this effect of illumination is attributable to a pigment absorbing near 585 nm (cf 568 for bacteriorhodopsin). Bleaching of the vesicles by prolonged illumination with hydroxylamine results in inactivation of the transport; retinal addition causes partial return of the activity. Retinal addition also causes the appearance of an absorption peak at 588 nm, while the absorption of free retinal decreases. The 588 nm pigment is present in very small quantities (0.13 nmole/mg protein), and behaves differently from bacteriorhodopsin in a number of respects. Vesicles can be prepared from bacteriorhodopsin-containing H halobium strains in which primary transport for both protons and sodium can be observed. Both pumps appear to cause the outward transport of the cations. The observations indicated the existence of a second retinal protein, addition to bacteriorhodopsin, in H halobium, which is associated with primary sodium translocation. The initial proton uptake normally observed during illumination of whole H halobium cells may therefore be a passive flux in response to the primary sodium extrusion.

Bacteriorhodopsins↗
PubMed1996

Two alternative models for spontaneous flagellar motor switching in Halobacterium salinarium.

Halobacteria are light-sensitive microorganisms which swim by means of rotating flagella. Under constant environmental conditions, they reverse their swimming direction about every 10-30 s. This is due to spontaneous switchings of the flagellar motors from clockwise to counterclockwise rotation or vice versa. However, it is unknown how the direction of rotation is regulated. In this paper, two stochastic models which could explain the characteristics of sequences of spontaneous switching events are discussed. The process is described in terms of a "motor switch" cyclically running through a sequence of states and triggering a reversal whenever a cycle is complete. Referring to previously stated hypotheses, modelling is based on the assumption that transitions between the states of the switch either occur with constant probability per unit time or are actively regulated by an endogenous biochemical oscillator. It is shown that both models yield a good description of the experimental data, though they are mutually exclusive.

Halobacterium↗
PubMed2002

On the aperiodic locomotor behavior of Halobacterium salinarium under periodic light stimuli.

Two long time series of swimming intervals of a bacterium inverting its motion under periodic light pulses are analysed. The associated next-period plots reveal, through their filiform structure, that the underlying dynamics are low-dimensional. Using recently described properties of such dynamics, a simple second-order black-box model for the swimming intervals is derived and validated. The model reinforces the conjecture that this bacterium is endowed with an oscillator controlling the switching of the flagellar motor.

Halobacterium salinarum↗
PubMed1977

Biogenesis of the purple membrane of Halobacterium halobium.

A protein closely resembling the purple membrane protein pre-exists in the cell membrane of H. halobium prior to the appearance of functional bacteriorhodopsin. It is associated with a differentiated membranous structure which has been isolated on a sucrose gradient and appears to be a precursor of the purple membrane. The identity of the precursor protein as a form of the purple membrane protein was established in different ways: (1) The cell proteins were labelled in vivo with 14C-proline during dark aerobic growth, the label was "chased", and the cells transferred to the illuminated near-anaerobic conditions under which purple membrane is optimally synthesised (induction conditions). Cell lysates were fractionated on sucrose gradients at different times after induction. Label first found in the precursor fraction appeared within 24 h in the purple membrane fraction. (2) SDS-urea-acrylamide gel electrophoresis of the purple membrane protein and the precursor showed only one protein band whose migration coincided with that of the purple membrane band. (3) The amino-acid analysis of the purified precursor was very similar to that of the purple membrane. The absorption spectrum of the precursor showed little of the characteristic absorption of bacteriorhodopsin at 570 nm. A major band appears at 412 nm, the exact nature of which is not known. The difference spectrum (reduced versus oxidised) of a purified fraction showed only traces of cytochrome. Thin-layer chromatography of an acetone-soluble lipid extract indicated the presence of retinal and beta-carotene. Cells grown in the presence of nicotine did not develop purple membrane after induction: the species absorbing at 412 nm was much less abundant than in non-inhibited cells, but a new fraction was present with a sharp peak at 345 nm consisting mainly of lycopene.

Bacteriorhodopsins↗
PubMed1978

Spectral transitions in purple membranes from Halobacterium halobium. I. Effect of preliminary illumination on photochemical processes.

The effect of preliminary illumination of purple membranes by yellow light on the difference spectra of short-lived intermediates has been studied. It has been found that changes of the optical density of two of these intermediates, which have the maxima of the difference spectrum at 412 nm and 650 nm, coincides well with the kinetics off the known reversible transitions of the main band of the purple membrane absorption (560 570), i.e., 13-cis-trans transitions. The changes at 412 nm and 650 nm are proportional to the concentration changes of the all-trans retinal and 13-cis retinal, respectively. It was concluded that the formation of the short-lived 412 and 650 intermediates occurs in different photochemical cycles. The pH is found to affect the formation of the 650 intermediate.

Bacteriorhodopsins↗