• Cytochrome C Oxidase

    Current traces of the Respiratory Chain Complex IV, known as Cytochrom c oxidase, measured on the SURFE²R N1

Cytochrome C Oxidase

Gene Family: Mitochondrial complex IV: cytochrome c oxidase subunits (COX, MT-CO)

The complex is a large integral membrane protein composed of several metal prosthetic sites and 14 protein subunits in mammals. Here, eleven subunits are nuclear in origin, and three are synthesized in the mitochondria. The complex contains two hemes, a cytochrome a and cytochrome a3, and two copper centers, the CuA and CuB centers.

The enzyme cytochrome c oxidase or electron transport chain (ETC) Complex IV is a large transmembrane protein complex found in bacteria and the mitochondrial membrane of eukaryotes. It receives an electron from each of four cytochrome c molecules, and transfers them to one oxygen molecule, converting molecular oxygen to two molecules of water. In the process, it binds four protons from the inner aqueous phase to make water and in addition translocates four protons across the membrane, in the process, helping to establish a transmembrane difference of proton electrochemical potential that the ATP synthase then uses to synthesize ATP.
Reaction: 4 Fe2+-cytochrome c + 8 H+in + O2 → 4 Fe3+-cytochrome c + 2 H2O + 4 H+out

Data and Applications

Respiratory Chain Complex IV - Current Traces

Surfer RC IVIcon N1   SURFE2R N1 data and applications:

The Respiratory Chain Complex IV, known as Cytochrom c oxidase, reduces oxygen by cunsumption of electrons from cytocrome c and transport of two protons to the intermembrans space. Here the reaction runs backwards.




2013 - Measuring Interference of Drug-Like Molecules with the Respiratory Chain: Toward the Early Identification of Mitochondrial Uncouplers in Lead Finding

Icon 96SE   SURFE²R N96 (predecessor model of SURFE²R 96SE) publication in Assay and Drug Development Technologies (2013)

Stock U., Matter H., Diekert K., Dörner W., Dröse S., Licher T.

2010 - Electrophysiology of respiratory chain complexes and the ADP-ATP exchanger in native mitochondrial membranes

Icon N1   SURFE²R ONE (a predecessor model of SURFE²R N1) publication in Biochemistry (2010)

Watzke N., Diekert K., Obrdlik P.

a.      P-bond hydrolysis driven transporters

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