Linked Life Data

2844533

Source:http://linkedlifedata.com/resource/pubmed/id/2844533

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-11-22
pubmed:abstractText
Analogue bacteriorhodopsins (BRs) were reconstituted from bacterioopsin and 9-, 11-, or 13-methoxyretinals or their demethyl derivatives, respectively. In organic solvents the retinals occur as cis isomers of the respective double bonds carrying the methoxy group. 9-Methoxyretinal, present as the 9-cis isomer, does not form an analogue BR with bacterioopsin in the dark. Upon illumination, a BR is produced with an absorbance maximum at 560 nm. This compound is thermally unstable, and converts back into the 9-cis-containing complex (lambda max = 410 nm) in the dark. Removal of the 13-methyl group from this compound (= 9-methoxy 13-demethyl retinal) does not change the 9-cis configuration of the free retinal, but allows the reconstitution of a thermally stable chromoprotein absorbing around 500 nm with a proton translocation rate of about 10% of the BR value, comparable to the 13-demethyl BR value [Gärtner, W., Towner, P., Hopf, H. & Oesterhelt, D. (1983) Biochemistry 22, 2637-2644]. 11-Methoxy BRs (13-demethyl and 9,13-didemethyl) absorb around 530 nm and are inactive. 13-Methoxy retinal (13-cis isomer) reconstitutes a chromoprotein with an absorbance maximum at 515 nm, which can be photoconverted to a thermostable 460-nm-absorbing complex. For the 515-nm-absorbing species of 13-methoxy BR a light-induced proton translocation was not detected in measurements with cell vesicles (detection of pH changes in the vesicle preparation). Only by photocurrent measurements in a bilayer experiment could a very diminished photocurrent be detected, about 1-2% of BR, [Fendler et al. (1987) Biochim. Biophys. Acta 893, 60-68]. The reconstitution rate of 13-methoxy BR from 13-methoxy retinal and bacterioopsin is slower by a factor of 40 compared to 13-ethyl BR, although both substituents are of similar size. The position 13 of retinal was found to be most sensitive for regulation of the absorption maximum and the formation and stability of the all-trans isomer, which is the active form for light-induced proton translocation. The results suggest that an electronic interaction with a charged residue of the binding site exists around position 13 of retinal, which is disturbed when a methoxy group replaces the methyl or ethyl group at that position. This electronic interaction is essential for maintaining the active all-trans configuration of retinal.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
641-8
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Methoxyretinals in bacteriorhodopsin. Absorption maxima, cis-trans isomerization and retinal protein interaction.
pubmed:affiliation
Institut für Biologie I (Zoologie), Freiburg, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't