Sökning: "Heme-copper oxidase"
Visar resultat 1 - 5 av 13 avhandlingar innehållade orden Heme-copper oxidase.
1. Experimental studies of proton translocation reactions in biological systems : Electrogenic events in heme-copper oxidases
Sammanfattning : Terminal heme-copper oxidases (HCuOs) are transmembrane proteins that catalyze the final step in the respiratory chain - the reduction of O2 to H2O, coupled to energy conservation by generation of an electrochemical proton gradient. The most extensively investigated of the HCuOs are the aa3-type oxidases, to which cytochrome c oxidase (CytcO) belongs, which uses energy released in the O2-reduction for proton pumping. LÄS MER
Sammanfattning : In the denitrification process where nitrate is stepwise reduced to nitrogen gas, the toxic molecule nitric oxide (NO) is formed as an intermediate. Nitric oxide is produced by the enzyme cd1 Nitrite reductase (cd1NiR) by reduction of nitrite and is later reduced to nitrous oxide by nitric oxide reductase (cNOR). LÄS MER
Sammanfattning : Heme-copper oxidases are transmembrane proteins that are found in aerobic and anaerobic respiratory chains. During aerobic respiration, these enzymes reduce dioxygen to water. The energy released in the reaction is used to transport protons across a biological membrane. LÄS MER
Sammanfattning : Heme-copper oxidases (HCuOs) are best known as terminal oxidases in the aerobic respiratory chain, in which they catalyze the reduction of oxygen to water. By receiving protons and electrons from opposite sides of the membrane as well as pumping protons, HCuOs contribute to the electrochemical proton gradient over the membrane that can be used for ATP synthesis. LÄS MER
Sammanfattning : In the last step of cellular respiration, electrons from metabolites are transferred to molecular oxygen, mediated by the enzyme complexes of the respiratory chain. Some of these enzyme complexes couple these redox reactions to formation of an electrochemical proton gradient across the cell membrane. The proton gradient is used e.g. LÄS MER