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 Lettjournal_title
FEBS lettersauthors
Perálvarez A,Barnadas R,Sabés M,Querol E,Padrós Edoi
10.1016/s0014-5793(01)03080-0keywords:
subject
Has Abstractpub_date
2001-11-23 00:00:00pages
399-402issue
3eissn
0014-5793issn
1873-3468pii
S0014-5793(01)03080-0journal_volume
508pub_type
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