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What is the coordination geometry and oxidation state of the metal ion in the active site of cytochrome c oxidase, an important metalloenzyme involved in the respiratory process of living organisms?

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Cytochrome c oxidase  CcO  is a metalloenzyme that plays a crucial role in the respiratory process of living organisms. The active site of CcO contains two metal ions: a copper ion  CuB  and a heme iron  Fea3 .The coordination geometry of the heme iron  Fea3  is typically square pyramidal. The iron is coordinated to a histidine residue, a porphyrin ring, and a water molecule or hydroxide ion. The copper ion  CuB  has a distorted tetrahedral coordination geometry, being coordinated to three histidine residues and a water molecule or hydroxide ion.The oxidation state of the heme iron  Fea3  in the active site of cytochrome c oxidase can vary between +2  ferrous  and +3  ferric  during the catalytic cycle. The copper ion  CuB  also undergoes redox changes, with its oxidation state varying between +1  cuprous  and +2  cupric .

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