Table of Contents
What is the role of cytochrome c oxidase?
Cytochrome c oxidase or complex IV, catalyzes the final step in mitochondrial electron transfer chain, and is regarded as one of the major regulation sites for oxidative phosphorylation. This enzyme is controlled by both nuclear and mitochondrial genomes.
What are the components of cytochrome c oxidase?
Cytochrome C oxidase (CCO) is composed of 13 protein subunits. It contains three copper ions, which are necessary for its function. It also contains zinc, magnesium, and two heme groups.
What is cytochrome oxidase and what is its action?
Cytochrome c oxidase is responsible for reduction of molecular oxygen to water using reducing equivalents donated by cytochrome c and for site 3 energy coupling in oxidative phosphorylation.
What is the role of superoxide dismutase?
Superoxide dismutases (SODs) constitute a very important antioxidant defense against oxidative stress in the body. The enzyme acts as a good therapeutic agent against reactive oxygen species-mediated diseases.
What activates superoxide dismutase?
The activity of each of the superoxide dismutase families relies upon a specific redox active metal ion, and depending on the SOD molecules, this could either be a manganese, iron, copper or nickel ion.
What is the function of an oxidase enzyme?
In biochemistry, an oxidase is an enzyme that catalyzes oxidation-reduction reactions, especially one involving dioxygen (O2) as the electron acceptor. In reactions involving donation of a hydrogen atom, oxygen is reduced to water (H2O) or hydrogen peroxide (H2O2).
What is COX deficiency?
Cytochrome C Oxidase (COX) deficiency is a very rare inherited metabolic disorder characterized by a deficiency of the enzyme cytochrome C oxidase or Complex IV. Cytochrome C oxidase is an essential enzyme that is active in subcellular structures that help to regulate energy production (mitochondria).
How does superoxide dismutase protect a cell?
Superoxide dismutases (SODs) are antioxidant enzymes that protect cells from toxic oxygen metabolites by converting superoxide into molecular oxygen and hydrogen peroxide via cyclic reduction and oxidation of an active site metal.
What reaction is catalyzed by cytochrome oxidase?
The reaction catalyzed by cytochrome oxidase is the four-electron reduction of O2 to water.
What happens without cytochrome c?
Approximately one-quarter of individuals with cytochrome c oxidase deficiency have a type of heart disease that enlarges and weakens the heart muscle (hypertrophic cardiomyopathy ). Another possible feature of this condition is an enlarged liver (hepatomegaly), which may lead to liver failure.
What is the role of cytochrome oxidase in the production of ATP?
Cytochrome oxidase is a transmembrane molecule found in the mitochondria of eukaryotes and in the cellular space of aerobic prokaryotes. This molecule is a proton pump that plays a vital role in producing energy, in the form of ATP, via the ETS (Figure 3).
Which is the inhibitor of cytochrome oxidase?
The four gases, nitric oxide (NO), carbon monoxide (CO), hydrogen sulfide (H(2)S) and hydrogen cyanide (HCN) all readily inhibit oxygen consumption by mitochondrial cytochrome oxidase. This inhibition is responsible for much of their toxicity when they are applied externally to the body.
What is the structure of cytochrome c oxidase?
Adapted from PDB: 1OCC (It is a homo dimer in this structure) The enzyme cytochrome c oxidase or Complex IV, EC 1.9.3.1, is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes. It is the last enzyme in the respiratory electron transport chain of cells located in the membrane.
What is mitochondrial cytochrome coxidase (Cox)?
A copper-containing metalloenzyme, mitochondrial cytochrome coxidase (COX), is the final electron acceptor in the mitochondrial electron transport chain and is required for aerobic ATP production. Over the last 15 years COX biogenesis has received significant attention because of its medical relevance.
Is cytochrome c oxidase a homo dimer?
Adapted from PDB: 1OCC (It is a homo dimer in this structure) The enzyme cytochrome c oxidase or Complex IV, EC 1.9.3.1, is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes.
What does carbon monoxide do to cytochrome c oxidase?
“Carbon monoxide specifically inhibits cytochrome c oxidase of human mitochondrial respiratory chain”. Pharmacology & Toxicology. 93 (3): 142–6. doi: 10.1034/j.1600-0773.2003.930306.x.