The bacteriorhodopsin proton pump: effect of crosslinkings of lysine residues.

Abstract:

:All six available lysine residues in bacteriorhodopsin were amidinated with dimethyl-3,3'-dithiobispropionimidate, which is a crosslinking agent. The photocycle was studied by measuring light absorption and electric signals. The data show an essential change in the photocycle: instead of single components, the rise of the signal due to the M intermediate can be decomposed into two components, and the decay into three. The life-times and the intensities of these components and in general the proton pumping activity of bacteriorhodopsin depend only negligibly upon pH. Changes upon removing the crosslinks are not significantly different from those in the crosslinked samples. The lysine residues therefore may not be considered of primary importance in proton translocation.

journal_name

Arch Biochem Biophys

authors

Tóth-Boconádi R,Taneva SG,Kiselev AV,Abdulaev NG,Keszthelyi L

doi

10.1016/0003-9861(88)90502-4

subject

Has Abstract

pub_date

1988-02-01 00:00:00

pages

725-31

issue

2

eissn

0003-9861

issn

1096-0384

pii

0003-9861(88)90502-4

journal_volume

260

pub_type

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