ferredoxin

Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.

Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. Adrenodoxin reductase Protein, Bovine, Recombinant (E. coli, His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 55.8 kDa and the accession number is P08165.

Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. FDXR Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 61.6 kDa and the accession number is P22570.

Essential for the synthesis of various steroid hormones. Participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage to produce pregnenolone, the precursor of most steroid hormones. Does not form a ternary complex with adrenodoxin reductase and CYP11A1 but shuttles between the two enzymes to transfer electrons. Adrenodoxin, mitochondrial Protein, Bovine, Recombinant (His) is expressed in E. coli expression system with N-10xHis tag. The predicted molecular weight is 19.5 kDa and the accession number is P00257.

Serves as the first electron transfer protein in all the mitochondrial P450 systems including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver. Adrenodoxin reductase Protein, Bovine, Recombinant (His) is expressed in yeast with N-10xHis tag. The predicted molecular weight is 52.8 kDa and the accession number is P08165.

Chlorite dismutase (Cld) found in prokaryotic organisms, also known as Chlorite O2-lyase, is a b-type heme containing enzyme that catalyzes the reduction of chlorite into chloride plus dioxygen. The subunit of chlorite dismutase consists of a heme free N-terminal and a heme b containing C-terminal ferredoxin-like fold with high structural homology to the dye-decolorizing peroxidases (DyPs). The physiological role of Cld in prokaryote has been shown that some microorganisms can use perchlorate or chlorate as terminal electron acceptors for anaerobic respiration thereby producing chlorite that must be detoxified. This enzyme has gained attention because it can be used in the development of bioremediation processes, biosensors, and controlled dioxygen production.