Direct measurement of picosecond charge separation in bacteriorhodopsin

G. I. Groma, G. Szabó, G. Váró

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

The Halobacterium halobium protein bacteriorhodopsin conservesthe energy of absorbed photons by converting it into a transmembrane proton gradient 1. Light absorption bybacteriorhodopsin is thought to drive a photocycle of intermediate states linked to the pumping of protons across the plasma membrane. The earliest intermediate of this photocycle so far detected is formed in 11-15 ps2,3, and this step could involve a separation of charges within the protein2,4-9. Although an electrical response signal with a time course correlating with that of the photocycle has been measured for bacteriorhodopsin, so far it has not been possible to resolve a signal corresponding to the initial charge separation10-16. We report here the resolution by picosecond laser spectroscopy of an electrical signal apparently corresponding to a charge separation with a time constant of approximately 30 ps, which we attribute to the formation of the first intermediate of the bacteriorhodopsin photocycle.

Original languageEnglish
Pages (from-to)557-558
Number of pages2
JournalNature
Volume308
Issue number5959
DOIs
Publication statusPublished - 1984

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polarization (charge separation)
protons
electromagnetic absorption
laser spectroscopy
time constant
pumping
membranes
proteins
gradients
photons
energy

ASJC Scopus subject areas

  • General

Cite this

Direct measurement of picosecond charge separation in bacteriorhodopsin. / Groma, G. I.; Szabó, G.; Váró, G.

In: Nature, Vol. 308, No. 5959, 1984, p. 557-558.

Research output: Contribution to journalArticle

Groma, G. I. ; Szabó, G. ; Váró, G. / Direct measurement of picosecond charge separation in bacteriorhodopsin. In: Nature. 1984 ; Vol. 308, No. 5959. pp. 557-558.
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