Ontology highlight
ABSTRACT:
SUBMITTER: Schulte M
PROVIDER: S-EPMC6560083 | biostudies-literature | 2019 Jun
REPOSITORIES: biostudies-literature
Schulte Marius M Frick Klaudia K Gnandt Emmanuel E Jurkovic Sascha S Burschel Sabrina S Labatzke Ramona R Aierstock Karoline K Fiegen Dennis D Wohlwend Daniel D Gerhardt Stefan S Einsle Oliver O Friedrich Thorsten T
Nature communications 20190611 1
Respiratory complex I plays a central role in cellular energy metabolism coupling NADH oxidation to proton translocation. In humans its dysfunction is associated with degenerative diseases. Here we report the structure of the electron input part of Aquifex aeolicus complex I at up to 1.8 Å resolution with bound substrates in the reduced and oxidized states. The redox states differ by the flip of a peptide bond close to the NADH binding site. The orientation of this peptide bond is determined by ...[more]