Catalytic intermediates of cytochrome bd terminal oxidase at steady-state: Ferryl and oxy-ferrous species dominate

Autor: Alessandro Giuffrè, Paolo Sarti, Elena Forte, Vitaliy B. Borisov

Publikováno v: Biochimica et Biophysica Acta (BBA)-Enzymology
Biochimica et Biophysica Acta (BBA)-Enzymology, Elsevier, 2011, 1807 (5), pp.503-9. <10.1016/j.bbabio.2011.02.007>
Biochimica et Biophysica Acta (BBA)-Enzymology, Elsevier, 2011, 1807 (5), pp.503-9. ⟨10.1016/j.bbabio.2011.02.007⟩

International audience; The cytochrome bd ubiquinol oxidase from Escherichia coli couples the exergonic two-electron oxidation of ubiquinol and four-electron reduction of O(2) to 2H(2)O to proton motive force generation by transmembrane charge separa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d0e560e67583fbbe12b0ed7e5029618
http://hdl.handle.net/11573/354607