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The features of cytochrome b5 reductase enzymes allow the successful reduction of molecules of cytochrome b5 to be used for various functions across the electron transport chain and metabolism. In metabolism, c5br is active in lipid conversion involving the elongation and desaturation of fatty acids and cholesterol biosynthesis.
The family of cytochrome b 5-like proteins includes (besides cytochrome b 5 itself) hemoprotein domains covalently associated with other redox domains in flavocytochrome cytochrome b 2 (L-lactate dehydrogenase; EC 1.1.2.3), sulfite oxidase (EC 1.8.3.1), plant and fungal nitrate reductases (EC 1.7.1.1, EC 1.7.1.2, EC 1.7.1.3), and plant and ...
These ubiquitous redox domains, in various combinations, are widely distributed in biological systems. FMN domain, ferredoxin or cytochrome b 5 transfer electrons between the flavin reductase (protein or domain) and P450. While P450-containing systems are found throughout all kingdoms of life, some organisms lack one or more of these redox domains.
A second electron is transferred, from either cytochrome P450 reductase, ferredoxins, or cytochrome b 5, reducing the Fe-O 2 adduct to give a short-lived peroxo state. The peroxo group formed in step 4 is rapidly protonated twice, releasing one molecule of water and forming the highly reactive species referred to as P450 Compound 1 (or just ...
The protein encoded by the CYB5R3 gene is cytochrome b5 reductase, a flavoprotein that is produced as two different isoforms with different localizations. There is an amphipathic microsomal isoform that is found in all cell types but red blood cells; this isoform has one hydrophobic membrane-anchoring domain and one catalytic domain that is ...
Cytochrome b is a protein found in the membranes of aerobic cells. In eukaryotic mitochondria (inner membrane) and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III (EC 1.10.2.2) — also known as the bc1 complex or ubiquinol-cytochrome c reductase.
NADH dehydrogenase → plastoquinol → b 6 f → cyt c 6 → cyt aa 3 → O 2. where the mobile electron carriers are plastoquinol and cytochrome c 6, while the proton pumps are NADH dehydrogenase, cyt b 6 f and cytochrome aa 3 (member of the COX3 family). Cyanobacteria are the only bacteria that produce oxygen during photosynthesis.
The structure of cytochrome b5 reductase, the enzyme that converts methemoglobin to hemoglobin. [1]Methemoglobin (British: methaemoglobin, shortened MetHb) (pronounced "met-hemoglobin") is a hemoglobin in the form of metalloprotein, in which the iron in the heme group is in the Fe 3+ state, not the Fe 2+ of normal hemoglobin.