Comparison of ubiquinol and cytochrome c terminal oxidases. An alternative view.

abstract

• 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 bo3-type ubiquinol oxidase from Escherichia coli and the cytochrome aa3-type cytochrome c oxidases. A second redox-active copper site (CuA) 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.

authors

• Musser, Siegfried

published proceedings

• FEBS Lett

author list (cited authors)

• Musser, S. M., Stowell, M. H., & Chan, S. I.

citation count

• 37

complete list of authors

• Musser, SM||Stowell, MH||Chan, SI

publication date

• July 1993

publisher

• Wiley  Publisher

published in

• FEBS Letters  Journal

keywords

• Bacteria
• Binding Sites
• Electron Transport
• Electron Transport Complex IV
• Proton Pumps
• Structure-Activity Relationship
• Substrate Specificity

PubMed Central ID

• 8392948

Digital Object Identifier (DOI)

• 10.1016/0014-5793(93)80156-o

start page

• 131

end page

• 136

volume

• 327

issue

• 2

URL

• http://dx.doi.org/10.1016/0014-5793(93)80156-o