Replacing Asn207 by Aspartate at the Neck of the D Channel in the aa(3)-type Cytochrome c Oxidase from Rhodobacter sphaeroides Results in Decoupling the Proton Pump

Lignende værker

• Decoupling mutations in the D-channel of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that a continuous hydrogen-bonded chain of waters is essential for proton pumping
  af: Zhu, Jiapeng, et al.
  Udgivet: (2010)
• Redox-coupled proton translocation in biological systems: Proton shuttling in cytochrome c oxidase
  af: Namslauer, Andreas, et al.
  Udgivet: (2003)
• Properties of Arg481 mutants of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a(3) is likely to be the proton loading site of the proton pump
  af: Lee, Hyun Ju, et al.
  Udgivet: (2009)
• Controlled uncoupling and recoupling of proton pumping in cytochrome c oxidase
  af: Brändén, Gisela, et al.
  Udgivet: (2006)
• The proton collecting function of the inner surface of cytochrome c oxidase from Rhodobacter sphaeroides
  af: Marantz, Yael, et al.
  Udgivet: (1998)