Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I

• DOI: 10.1073/pnas.1714074114
• Publication Date: 2017-11-13T19:50:51Z
• Authors: Justin G. Fedor; Andrew J. Y. Jones; Andrea Di Luca; Ville R. I. Kaila; Judy Hirst
• Keywords: Mitochondrial respiratory chain

Significance Respiratory complex I, a redox-coupled proton pumping enzyme, is central to aerobic metabolism in mammalian mitochondria and implicated many neuromuscular disorders. One of its substrates, ubiquinone-10, binds an unusually long narrow channel, which at the intersection enzyme’s electron transfer modules hotspot for disease-causing mutations. Here, we use minimal, self-assembled respiratory chain study I catalyzing with ubiquinones different isoprenoid lengths. We show that channel enhances affinity long-chain quinones, assists their along organizes them product release. Finally, discuss how efficient binding dissociation processes may help link redox catalysis energy conversion.