Simulating the slow to fast switch in cytochrome c oxidase catalysis by introducing a loop flip near the enzyme's cytochrome c (substrate) binding site

The mitochondrial enzyme cytochrome c oxidase catalyzes the reduction of molecular oxygen in the critical step of oxidative phosphorylation that links the oxidation of food consumed to ATP production in cells. The enzyme catalyzes the reduction of oxygen at two vastly different rates that are though...

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Veröffentlicht in:	Biotechnology and applied biochemistry 2017-09, Vol.64 (5), p.677-685
Hauptverfasser:	Alleyne, Trevor, Ignacio, Diane N., Sampson, Valerie B., Ashe, Damian, Wilson, Michael
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Animals Binding sites Binding Sites - genetics Catalysis Cattle charge/hydride relay Conformation conformational change Cytochrome cytochrome c Cytochrome-c oxidase Cytochromes c - chemistry Cytochromes c - metabolism Electron transfer Electron Transport Complex IV - chemistry Electron Transport Complex IV - genetics Electron Transport Complex IV - metabolism Electrons Enzymes ES complex Food production Haem Hydrogen Bonding Hydrogen storage loop flip Lysine Mitochondria Mitochondrial DNA Models, Molecular Oxidase Oxidation Oxidative phosphorylation Oxygen Phosphorylation Protein Conformation Proteins Reduction Relay systems Residues resting/pulsed oxidase Simulation
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