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Comparison of ubiquinol and cytochrome c terminal oxidases
Author(s) -
Musser Siegfried M.,
Stowell Michael H.B.,
Chan Sunney I.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80156-o
Subject(s) - ubiquinol , chemistry , cytochrome , cytochrome c , terminal (telecommunication) , biochemistry , stereochemistry , coenzyme q – cytochrome c reductase , enzyme , mitochondrion , computer science , telecommunications
There have been numerous instances in the recent literature where the properties of ubiquinol and cytochrome c terminal oxidases are compared. Here we specifically examine the cytochrome bo 3 ‐type ubiquinol oxidase from Escherichia coli and the cytochrome aa 3 ‐type cytochrome c oxidases. A second redox‐active copper site (Cu A ) is present only in the cytochrome c oxidases and the physiological electron donors for the two enzymes are different (ubiquinol‐8 vs. ferrocytochrome c ). In our opinion, these differences are significant and most likely indicate that distinct turnover mechanisms are operative in the two enzymes.