Topic
Quinone binding
About: Quinone binding is a research topic. Over the lifetime, 295 publications have been published within this topic receiving 9379 citations.
Papers published on a yearly basis
Papers
TL;DR: Observed rates of superoxide generation by rat skeletal muscle mitochondria under a variety of conditions suggest that quinone-binding site inhibitors can make complex I adopt the highly radical-producing state that occurs during reverse electron transport.
500 citations
TL;DR: The first structure of a ubiquinol oxidase, cy tochrome bo3, from Escherichia coli is reported, which contains a cluster of polar residues exposed to the interior of the lipid bilayer that is not present in the cytochrome c oxidase.
Abstract: Cell respiration is catalyzed by the heme-copper oxidase superfamily of enzymes, which comprises cytochrome c and ubiquinol oxidases. These membrane proteins utilize different electron donors through dissimilar access mechanisms. We report here the first structure of a ubiquinol oxidase, cytochrome bo3, from Escherichia coli. The overall structure of the enzyme is similar to those of cytochrome c oxidases; however, the membrane-spanning region of subunit I contains a cluster of polar residues exposed to the interior of the lipid bilayer that is not present in the cytochrome c oxidase. Mutagenesis studies on these residues strongly suggest that this region forms a quinone binding site. A sequence comparison of this region with known quinone binding sites in other membrane proteins shows remarkable similarities. In light of these findings we suggest specific roles for these polar residues in electron and proton transfer in ubiquinol oxidase.
414 citations
TL;DR: The proton‐pumping NADH:ubiquinone oxidoreductase, also called complex I, is the first of the respiratory complexes providing the proton motive force which is essential for energy consuming processes like the synthesis of ATP.
366 citations
TL;DR: A mechanism for the reduction of ubiquinone during the catalytic turnover of the enzyme SQR is proposed, and two binding positions are proposed for the E. coli SQR quinone-binding site to explain these data.
287 citations
TL;DR: A structure-based summary of inter-heme distances in seven bc complexes, representing mitochondrial, chromatophore, cyanobacterial, and algal sources, indicates that, based on the distance parameter, the intra-monomer pathway would be favored kinetically.
181 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2021 | 7 |
| 2020 | 5 |
| 2019 | 3 |
| 2018 | 4 |
| 2017 | 5 |
| 2016 | 9 |