Direct Demonstration of Half-of-the-sites Reactivity in the Dimeric Cytochrome bc(1) Complex: ENZYME WITH ONE INACTIVE MONOMER IS FULLY ACTIVE BUT UNABLE TO ACTIVATE THE SECOND UBIQUINOL OXIDATION SITE IN RESPONSE TO LIGAND BINDING AT THE UBIQUINONE REDUCTION SITE

Gelijkaardige items

• The Rate-limiting Step in the Cytochrome bc(1) Complex (Ubiquinol-Cytochrome c Oxidoreductase) Is Not Changed by Inhibition of Cytochrome b-dependent Deprotonation: IMPLICATIONS FOR THE MECHANISM OF UBIQUINOL OXIDATION AT CENTER P OF THE bc(1) COMPLEX
  door: Covian, Raul, et al.
  Gepubliceerd in: (2009)
• Ilicicolin Inhibition and Binding at Center N of the Dimeric Cytochrome bc(1) Complex Reveal Electron Transfer and Regulatory Interactions between Monomers
  door: Covian, Raul, et al.
  Gepubliceerd in: (2009)
• The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Restoration of ubiquinone-pool behaviour.
  door: Heron, C, et al.
  Gepubliceerd in: (1978)
• Membrane Potential Greatly Enhances Superoxide Generation by the Cytochrome bc(1) Complex Reconstituted into Phospholipid Vesicles
  door: Rottenberg, Hagai, et al.
  Gepubliceerd in: (2009)
• Reaction Mechanism of Superoxide Generation during Ubiquinol Oxidation by the Cytochrome bc(1) Complex
  door: Yin, Ying, et al.
  Gepubliceerd in: (2010)