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  2. Cytochrome b5 reductase - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_b5_reductase

    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 ...

  3. CYB5R3 - Wikipedia

    en.wikipedia.org/wiki/CYB5R3

    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 ...

  4. Cytochrome b5 - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_b5

    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 ...

  5. P450-containing systems - Wikipedia

    en.wikipedia.org/wiki/P450-containing_systems

    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.

  6. Methemoglobin - Wikipedia

    en.wikipedia.org/wiki/Methemoglobin

    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.

  7. Cytochrome b - Wikipedia

    en.wikipedia.org/wiki/Cytochrome_b

    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.

  8. Fatty acid synthesis - Wikipedia

    en.wikipedia.org/wiki/Fatty_acid_synthesis

    In mammals the aerobic desaturation is catalyzed by a complex of three membrane-bound enzymes (NADH-cytochrome b 5 reductase, cytochrome b 5, and a desaturase). These enzymes allow molecular oxygen, O 2, to interact with the saturated fatty acyl-CoA chain, forming a double bond and two molecules of water, H 2 O. Two electrons come from NADH + H +

  9. Cytochrome - Wikipedia

    en.wikipedia.org/wiki/Cytochrome

    Complex IV contains a cytochrome a/a3-domain that transfers electrons and catalyzes the reaction of oxygen to water. Photosystem II, the first protein complex in the light-dependent reactions of oxygenic photosynthesis, contains a cytochrome b subunit. Cyclooxygenase 2, an enzyme involved in inflammation, is a cytochrome b protein.