Ontology highlight
ABSTRACT:
SUBMITTER: Kyndt JA
PROVIDER: S-EPMC3322269 | biostudies-literature | 2012 May
REPOSITORIES: biostudies-literature
Kyndt John A JA Fitch John C JC Berry Robert E RE Stewart Matt C MC Whitley Kevin K Meyer Terry E TE Walker F Ann FA Cusanovich Michael A MA
Biochimica et biophysica acta 20120128 5
A triad of tyrosine residues (Y152-154) in the cytochrome c(1) subunit (C1) of the Rhodobacter capsulatus cytochrome bc(1) complex (BC1) is ideally positioned to interact with cytochrome c(2) (C2). Mutational analysis of these three tyrosines showed that, of the three, Y154 is the most important, since its mutation to alanine resulted in significantly reduced levels, destabilization, and inactivation of BC1. A second-site revertant of this mutant that regained photosynthetic capacity was found t ...[more]