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Insights into the ubiquinol/dioxygen binding and proton relay pathways of the alternative oxidase.
- Source :
-
Biochimica et biophysica acta. Bioenergetics [Biochim Biophys Acta Bioenerg] 2019 May 01; Vol. 1860 (5), pp. 375-382. Date of Electronic Publication: 2019 Mar 22. - Publication Year :
- 2019
-
Abstract
- The alternative oxidase (AOX) is a monotopic diiron carboxylate protein which catalyzes the four-electron reduction of dioxygen to water by ubiquinol. Although we have recently determined the crystal structure of Trypanosoma brucei AOX (TAO) in the presence and absence of ascofuranone (AF) derivatives (which are potent mixed type inhibitors) the mechanism by which ubiquinol and dioxygen binds to TAO remain inconclusive. In this article, ferulenol was identified as the first competitive inhibitor of AOX which has been used to probe the binding of ubiquinol. Surface plasmon resonance reveals that AF is a quasi-irreversible inhibitor of TAO whilst ferulenol binding is completely reversible. The structure of the TAO-ferulenol complex, determined at 2.7 Å, provided insights into ubiquinol binding and has also identified a potential dioxygen molecule bound in a side-on conformation to the diiron center for the first time.<br /> (Crown Copyright © 2019. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Coumarins chemistry
Mitochondrial Proteins metabolism
Oxidoreductases metabolism
Oxygen metabolism
Plant Proteins metabolism
Protozoan Proteins metabolism
Surface Plasmon Resonance
Ubiquinone chemistry
Ubiquinone metabolism
Mitochondrial Proteins chemistry
Oxidoreductases chemistry
Oxygen chemistry
Plant Proteins chemistry
Protozoan Proteins chemistry
Trypanosoma brucei brucei enzymology
Ubiquinone analogs & derivatives
Subjects
Details
- Language :
- English
- ISSN :
- 1879-2650
- Volume :
- 1860
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta. Bioenergetics
- Publication Type :
- Academic Journal
- Accession number :
- 30910528
- Full Text :
- https://doi.org/10.1016/j.bbabio.2019.03.008