|Title||Cryo-EM structures of intermediates suggest an alternative catalytic reaction cycle for cytochrome c oxidase.|
|Journal, issue, pages||Nat Commun, Vol. 12, Issue 1, Page 6903, Year 2021|
|Publish date||Nov 25, 2021|
|Authors||F Kolbe / S Safarian / Ż Piórek / S Welsch / H Müller / H Michel /|
|PubMed Abstract||Cytochrome c oxidases are among the most important and fundamental enzymes of life. Integrated into membranes they use four electrons from cytochrome c molecules to reduce molecular oxygen (dioxygen) ...Cytochrome c oxidases are among the most important and fundamental enzymes of life. Integrated into membranes they use four electrons from cytochrome c molecules to reduce molecular oxygen (dioxygen) to water. Their catalytic cycle has been considered to start with the oxidized form. Subsequent electron transfers lead to the E-state, the R-state (which binds oxygen), the P-state (with an already split dioxygen bond), the F-state and the O-state again. Here, we determined structures of up to 1.9 Å resolution of these intermediates by single particle cryo-EM. Our results suggest that in the O-state the active site contains a peroxide dianion and in the P-state possibly an intact dioxygen molecule, the F-state may contain a superoxide anion. Thus, the enzyme's catalytic cycle may have to be turned by 180 degrees.|
|External links||Nat Commun / PubMed:34824221 / PubMed Central|
|Methods||EM (single particle)|
|Resolution||2.4 - 2.66 Å|
|Keywords||MEMBRANE PROTEIN / Terminal oxidase Cytochrome c oxidase aa3 oxidase|
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