p-Hydroxybenzoate hydroxylase (PHBH) catalyzes the oxygenation of p-hydroxybenzoate (pOHB) to 3,4-dihyroxybenzoate (3,4-diOHB); FAD, NADPH and molecular oxygen are all required for this reaction.
NADPH first transfers a hydride equivalent to FAD, creating FADH⁻, and then NADP⁺ dissociates from the enzyme.
Reduced PHBH then reacts with molecular oxygen to form the flavin-C(4a)-hydroperoxide.
The flavin hydroperoxide quickly hydroxylates pOHB, and then eliminates water to regenerate oxidized flavin.
An alternative flavin-mediated oxygenation mechanism involves the use of a flavin-N(5)-oxide rather than a flavin-C(4a)-(hydro)peroxide.
p-Hydroxybenzoate hydroxylase (PHBH) catalyzes the oxygenation of p-hydroxybenzoate (pOHB) to 3,4-dihyroxybenzoate (3,4-diOHB); FAD, NADPH and molecular oxygen are all required for this reaction. NADPH first transfers a hydride equivalent to FAD, creating FADH⁻, and then NADP⁺ dissociates from the enzyme. Reduced PHBH then reacts with molecular oxygen to form the flavin-C(4a)-hydroperoxide. The flavin hydroperoxide quickly hydroxylates pOHB, and then eliminates water to regenerate oxidized flavin. An alternative flavin-mediated oxygenation mechanism involves the use of a flavin-N(5)-oxide rather than a flavin-C(4a)-(hydro)peroxide.
Flavin adenine dinucleotide