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- Title
Substitution of isoleucine L177 by histidine in Rhodobacter sphaeroides reaction center results in the covalent binding of P<sub>A</sub> bacteriochlorophyll to the L subunit
- Authors
Fufina, Tatiana Y.; Vasilieva, Lyudmila G.; Khatypov, Ravil A.; Shkuropatov, Anatoly Ya.; Shuvalov, Vladimir A.
- Abstract
Abstract: In this work, we report the unique case of bacteriochlorophyll (BChl) – protein covalent attachment in a photosynthetic membrane complex caused by a single mutation. The isoleucine L177 was substituted by histidine in the photosynthetic reaction center (RC) of Rhodobacter sphaeroides. Pigment analysis revealed that one BChl molecule was missing in the acetone–methanol extract of the I(L177)H RCs. SDS–PAGE demonstrated that this BChl molecule could not be extracted with organic solvents apparently because of its stable covalent attachment to the mutant RC L-subunit. Our data indicate that the attached bacteriochlorophyll is one of the special pair BChls, PA. The chemical nature of this covalent interaction remains to be identified.
- Subjects
PHOTOSYNTHETIC reaction centers; GENETIC mutation; ORGANIC solvents; CHLOROPHYLL
- Publication
FEBS Letters, 2007, Vol 581, Issue 30, p5769
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.11.032