Premium
Substitution of isoleucine L177 by histidine in Rhodobacter sphaeroides reaction center results in the covalent binding of P A bacteriochlorophyll to the L subunit
Author(s) -
Fufina Tatiana Y.,
Vasilieva Lyudmila G.,
Khatypov Ravil A.,
Shkuropatov Anatoly Ya.,
Shuvalov Vladimir A.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.032
Subject(s) - bacteriochlorophyll , rhodobacter sphaeroides , photosynthetic reaction centre , chemistry , covalent bond , histidine , stereochemistry , isoleucine , photochemistry , molecule , photosynthesis , biochemistry , amino acid , organic chemistry , leucine , electron transfer
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, P A . The chemical nature of this covalent interaction remains to be identified.