Article
Tyrosine triad at the interface between the Rieske iron-sulfur protein, cytochrome c1 and cytochrome c2 in the bc1 complex of Rhodobacter capsulatus.
Biochimica et biophysica acta - 1 May 2012
Kyndt John A, Fitch John C, Berry Robert E, Stewart Matt C, Whitley Kevin, Meyer Terry E, Walker F Ann, Cusanovich Michael A
Abstract excerpt
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...
Topics
- Amino Acid Sequence
- Animals
- Biocatalysis
- Cytochromes c1
- Cytochromes c2
- Electron Transport Complex III
- Electrophoresis, Polyacrylamide Gel
- Heme
- Models, Molecular
- Molecular Sequence Data