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Deoxyhemoglobin PDB coordinates, Brookhaven Protein Data Bank.

GSH is used as a cofactor by (1) multiple peroxidase enzymes, to detoxify peroxides generated from oxygen radical attack on biological molecules; (2) transhydrogenases, to reduce oxidized centers on DNA, proteins, and other biomolecules; and (3) glutathione S-transferases (GST) to conjugate GSH with endogenous substances (e.g., estrogens), exogenous electrophiles (e.g., arene oxides, unsaturated carbonyls, organic halides), and diverse xenobiotics. Low GST activity may increase risk for disease—but paradoxically, some GSH conjugates can also be toxic.

Sulfur is a component of biotin, insulin, glutathione, thiamine, coenzyme A.

In some of the proteins you have seen already, there have been other molecules bound, either covalently or noncovalently, to the proteins. These accessory molecules are called cofactors, and do specific things to help the proteins carry out their functions. For example, in hemoglobin (lower left), the cofactor heme binds the oxygen that is transported from the lungs to the other tissues of the body; the second image is zoomed in on one of the heme molecules. In alcohol dehydrogenase (third image), which is responsible for oxidizing alcohol to acetate in the liver, the cofactors nicotinamide adenine diphosphate (NAD), dimethyl sulfoxide (DMS) and Zn2+ work together to remove electrons from molecules of alcohol. The final image shows a close-up of the NAC, DMS and Zn2+ cofactors.

Oxyhemoglobin PDB coordinates, Brookhaven Protein Data Bank.

Clinical Context: Folic acid is an important cofactor for enzymes used in the production of red blood cells (RBCs).

Coenzyme Q10 (CoQ10), also known as ubiquinone, is an endogenously produced lipid-soluble cofactor that has a significant role in the formation of energy within cells. It also serves as a potent antioxidant and is very effective in inhibiting the oxidation and modification of low density lipoproteins (LDLs). In addition to endogenous production, dietary sources and/or supplements provide CoQ10. Reflects the amount of CoQ10 present in serum.

Vitamin B12 is required for proper red blood cell formation, neurological function, and DNA synthesis. Vitamin B12 also functions as a cofactor for homocysteine metabolism.

What mineral is a cofactor in the formation of hemoglobin?

Manganese helps produce mucopolysaccharides, stimulates the production of cholesterol and is a co-factor in many of the body's enzymes.

Cofactor in enzymatic systems involved in the metabolism of carbohydrates, fats, proteins, sulfur-containing amino acids, nucleic acids (DNA, RNA) and iron.

GSH is the essential cofactor for many enzymes that require thiol-reducing equivalents, and helps keep redox-sensitive active sites on enzyme in the necessary reduced state. Higher-order thiol cell systems, the metallothioneins, thioredoxins and other redox regulator proteins are ultimately regulated by GSH levels—and the GSH/GSSG redox ratio. GSH/GSSG balance is crucial to homeostasis—stabilizing the cellular biomolecular spectrum, and facilitating cellular performance and survival.

Which mineral is a cofactor for hemoglobin synthesis
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Cofactors, Coenzymes and Prosthetic group | …

Vitamin B-12 and folate coenzymes are required for thymidylate and purine synthesis; thus, their deficiency results in retarded DNA synthesis. In vitamin B-12 deficiency and folic acid deficiency, the defect in DNA synthesis affects other rapidly dividing cells as well, which may be manifested as glossitis, skin changes, and flattening of intestinal villi.

Cofactors, Coenzymes and Prosthetic group

Vitamin B-12 deficiency is a cause of macrocytosis. Because DNA synthesis requires cyanocobalamin (vitamin B-12) as a cofactor, a deficiency of the vitamin leads to decreased DNA synthesis in the erythrocyte, thus resulting in macrocytosis. A dietary deficiency of vitamin B-12 is rare and usually only occurs in elderly persons on a "tea-and-toast diet" or in strict vegan vegetarians. However, deficiency can result from the following:

although the precise role varies with the cofactor and the enzyme.

GSH equivalents circulate in the blood predominantly as cystine, the oxidized and more stable form of cysteine. Cells import cystine from the blood, reconvert it to cysteine (likely using ascorbate as cofactor), and from it synthesize GSH. Conversely, inside the cell, GSH helps re-reduce oxidized forms of other antioxidants—such as ascorbate and alpha-tocopherol.

A prosthetic group and cofactor

1The coordinates for the hemoglobin protein were determined using x-ray crystallography, and the image was rendered using SwissPDB Viewer and POV-Ray.
To view the molecules interactively, please use .

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