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  2. Cytochrome c oxidase - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_c_oxidase

    The fourth electron from another cytochrome c flows through Cu A and cytochrome a to the cytochrome a 3 –Cu B binuclear center, reducing the Fe 4+ =O to Fe 3+, with the oxygen atom picking up a proton simultaneously, regenerating this oxygen as a hydroxide ion coordinated in the middle of the cytochrome a 3 –Cu B center as it was at the ...

  3. COX17 - Wikipedia

    en.wikipedia.org/wiki/COX17

    Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen.This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes.

  4. Cytochrome c - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_c

    Cytochrome c is a highly conserved protein across the spectrum of eukaryotic species, found in plants, animals, fungi, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), [7] makes it useful in studies of cladistics. [8] Cytochrome c has been studied for the glimpse it gives into evolutionary ...

  5. Copper protein - Wikipedia

    en.wikipedia.org/wiki/Copper_protein

    Binuclear Copper A centres (Cu A) are found in cytochrome c oxidase and nitrous-oxide reductase (EC 1.7.99.6). The two copper atoms are coordinated by two histidines, one methionine, a protein backbone carbonyl oxygen, and two bridging cysteine residues. [7] Copper B centres (Cu B) are found in cytochrome c oxidase. The copper atom is ...

  6. Heme C - Wikipedia

    en.wikipedia.org/wiki/Heme_C

    The redox potential for cytochrome c can also be "fine-tuned" by small changes in protein structure and solvent interaction. [4] The number of heme C units bound to a holoprotein is highly variable. For vertebrate cells one heme C per protein is the rule but for bacteria this number is often 2, 4, 5, 6 or even 16 heme C groups per holoprotein.

  7. Oxidase - Wikipedia

    en.wikipedia.org/wiki/Oxidase

    An important example is EC 7.1.1.9 cytochrome c oxidase, the key enzyme that allows the body to employ oxygen in the generation of energy and the final component of the electron transfer chain. Other examples are: EC 1.1.3.4 Glucose oxidase; EC 1.4.3.4 Monoamine oxidase; EC 1.14.-.- Cytochrome P450 oxidase; EC 1.6.3.1 NADPH oxidase

  8. COX5B - Wikipedia

    en.wikipedia.org/wiki/COX5B

    Cytochrome c oxidase (COX) is the terminal enzyme of the mitochondrial respiratory chain. It is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane to drive ATP synthesis via protonmotive force.

  9. Oxidative phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Oxidative_phosphorylation

    Cytochrome c oxidase, also known as complex IV, is the final protein complex in the electron transport chain. [40] The mammalian enzyme has an extremely complicated structure and contains 13 subunits, two heme groups, as well as multiple metal ion cofactors – in all, three atoms of copper , one of magnesium and one of zinc .