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The specialized protein cytochrome b5 is a class B cytochrome with a high and low potential heme b attached to the central iron on the protein. [4] The cytochrome b class is especially unique because it is attached to proteins within the inner mitochondrial membrane instead of on the outer portion, and this particular class has high sequence ...
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.
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.
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 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.
72017 Ensembl ENSG00000159348 ENSMUSG00000026456 UniProt Q9UHQ9 Q9DB73 RefSeq (mRNA) NM_016243 NM_028057 NM_001355133 RefSeq (protein) NP_057327 NP_082333 NP_001342062 Location (UCSC) Chr 1: 202.96 – 202.97 Mb Chr 1: 134.33 – 134.34 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse NADH-cytochrome b5 reductase 1 is an enzyme that in humans is encoded by the CYB5R1 gene. Structure ...