Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding.

ABSTRACT: Bovine cytochrome c oxidase is an integral membrane protein complex comprising 13 protein subunits and associated lipids. Dimerization of the complex has been proposed; however, definitive evidence for the dimer is lacking. We used advanced mass spectrometry methods to investigate the oligomeric state of cytochrome c oxidase and the potential role of lipids and posttranslational modifications in its subunit interfaces. Mass spectrometry of the intact protein complex revealed that both the monomer and the dimer are stabilized by large lipid entities. We identified these lipid species from the purified protein complex, thus implying that they interact specifically with the enzyme. We further identified phosphorylation and acetylation sites of cytochrome c oxidase, located in the peripheral s

SUBMITTER: Liko I 

PROVIDER: S-EPMC4961149 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature