L-gulonolactone oxidase L-gulonolactone oxidase -gulonolactone oxidase (EC 1.1.3.8) is an enzyme that produces vitamin C, but is non-functional in Haplorrhini (including humans), in some bats, and in guinea pigs. It catalyzes the reaction of -gulono-1,4-lactone with oxygen to -xylo-hex-3-gulonolactone and hydrogen peroxide. It uses FAD as a cofactor. The -xylo-hex-3-gulonolactone (2-keto-gulono-gamma-lactone) is able to convert to hexuronic acid (ascorbic acid) spontaneously, without enzymatic action. The non-functional gulonolactone oxidase pseudogene (GULOP) was mapped to human chromosome 8p21 that corresponds to an evolutionarily conserved segment on either porcine chromosome 4 (SSC4) or 14 (SSC14). GULO produces the precursor to ascorbic acid, which spontaneously converts
Nucleic acid structure determination short lived in solution they need to be generated. This can be done using HO, ascorbic acid, and Fe(II)-EDTA complex which is attached to the backbone through EDTA. The Fe(II) along with ascorbic acid generates hydroxyl radicals which then can react with the nucleic acid molecules. Hydroxyl radical probing is often used in conjunction with chemical probing of nucleic acid molecules that are thought to associate with proteins, this is due to the modification done by hydroxyl radicals. Hydroxyl radicals attack the ribose/deoxyribose ring and this results in breaking of the phosphate backbone, which is independent of secondary structure, as