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Consurf Activity Cytochrome C

Ben Ernest, Joel Bucci, Letitia Olson

Cytochrome C oxidase is an enzyme in the electron transport chain that catalyzes electron transfer to reduce oxygen to water.  This reaction produces protons, which are then used to power the ATP synthases

Axel Harrenga and Hartmut Michel. The Cytochrome c Oxidase from Paracoccus denitrificans Does Not Change the Metal Center Ligation upon Reduction. J Biol Chem, Vol. 274, Issue 47, 33296-33299, November 19, 1999

Paracoccus Denitrificans

Aligned against:
Rhodobacter sphaeroides
Rhizobium leguminosarum
Rickettsia felis
Rickettsia bellii
Rickettsia prowazekii
Rickettsia conorii
Marchantia polymorpha
Beta vulgaris
Bradyrhizobium japonicum
Zea mays
Aegilops columnaris
Arabidopsis thaliana
Prototheca wickerhamii
Glycine max
Cyanidium caldarium
Pisum sativum
Chondrus crispus
Oenothera bertiana
Acanthamoeba castellanii
Ustilago maydis
Phytophthora megasperma
Metridium senile
Emericella nidulans
Neurospora crassa



Degree of conservation is high in the interior of the protein and more variable on the surface.   More specifically, the copper-binding site (indicated by the arrow), which is essential for protein function, due to its role in accepting electrons, is very highly conserved.

Is the copper binding site the active site?
How does protein structure change when copper is reduced?

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