Thr90 is a key residue of the bacteriorhodopsin proton pumping mechanism.

Abstract:

:Mutation of Thr90 to Ala has a profound effect on bacteriorhodopsin properties. T90A shows about 20% of the proton pumping efficiency of wild type, once reconstituted into liposomes. Mutation of Thr90 influences greatly the Schiff base/Asp85 environment, as demonstrated by altered lambda(max) of 555 nm and pK(a) of Asp85 (about 1.3 pH units higher than wild type). Hydroxylamine accessibility is increased in both dark and light and differential scanning calorimetry and visible spectrophotometry show decreased thermal stability. These results suggest that Thr90 has an important structural role in both the unphotolysed bacteriorhodopsin and in the proton pumping mechanism.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Perálvarez A,Barnadas R,Sabés M,Querol E,Padrós E

doi

10.1016/s0014-5793(01)03080-0

keywords:

subject

Has Abstract

pub_date

2001-11-23 00:00:00

pages

399-402

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)03080-0

journal_volume

508

pub_type

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