Inositol Oxygenase
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Inositol Oxygenase
Inositol oxygenase, also commonly referred to as ''myo-''inositol oxygenase (MIOX), is a non-heme di-Iron#Biological role, iron enzyme that oxidizes myo-inositol, ''myo''-inositol to glucuronic acid. The enzyme employs a unique four-electron transfer at its Fe(II)/Fe(III) coordination sites and the reaction proceeds through the direct binding of ''Myo-inositol, myo''Myo-inositol, -inositol followed by attack of the iron center by diatomic oxygen. This enzyme is part of the only known pathway for the catabolism of inositol in humans and is expressed primarily in the kidneys. Recent medical research regarding MIOX has focused on understanding its role in metabolic and kidney diseases such as diabetes, obesity and acute kidney injury. Industrially-focused engineering efforts are centered on improving MIOX activity in order to produce Saccharic acid, glucaric acid in heterologous hosts. Structure ''Myo''-inositol oxygenase is a monomeric 33 Atomic mass unit, kDa protein in both sol ...
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Heme
Heme, or haem (pronounced / hi:m/ ), is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver. In biochemical terms, heme is a coordination complex "consisting of an iron ion coordinated to a porphyrin acting as a tetradentate ligand, and to one or two axial ligands." The definition is loose, and many depictions omit the axial ligands. Among the metalloporphyrins deployed by metalloproteins as prosthetic groups, heme is one of the most widely used and defines a family of proteins known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase. The word ''haem'' is derived from Greek ''haima'' meaning "blood". Function Hemoproteins have diverse biological functions incl ...
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