The involvement of threonine 160 of cytochrome b of Rhodobacter sphaeroides cytochrome bc1 complex in quinone binding and interaction with subunit IV.

Abstract excerpt

The cytochrome b subunit (subunit I) of the ubiquinolcytochrome c reductase (bc1 complex) is thought to participate in the formation of two quinone/quinol reaction centers, an oxidizing center (Qo) and a reducing center, in accordance with the quinone cycle mechanism. Threonine 160 is a highly conserved residue in a segment of subunit I that was shown to bind quinone and is placed near the putative Qo site in...

Topics

• Antimycin A
• Base Sequence
• Benzoquinones
• Cytochrome b Group
• Electron Spin Resonance Spectroscopy
• Electron Transport Complex III
• Iron-Sulfur Proteins
• Molecular Sequence Data
• Mutagenesis, Site-Directed
• Mutation