Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy.

ABSTRACT: Although internal electron transfer and oxygen reduction chemistry in cytochrome c oxidase are fairly well understood, the associated groups and pathways that couple these processes to gated proton translocation across the membrane remain unclear. Several possible pathways have been identified from crystallographic structural models; these involve hydrophilic residues in combination with structured waters that might reorganize to form transient proton transfer pathways during the catalytic cycle. To date, however, comparisons of atomic structures of different oxidases in different redox or ligation states have not provided a consistent answer as to which pathways are operative or the details of their dynamic changes during catalysis. In order to provide an experimental means to address thi

SUBMITTER: Marechal A 

PROVIDER: S-EPMC3102355 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature