3-HYDROXYBENZOATE 6-HYDROXYLASE FROM PSEUDOMONAS-AERUGINOSA
3-HYDROXYBENZOATE 6-HYDROXYLASE FROM PSEUDOMONAS-AERUGINOSA
复制标题
DOI：
10.1016/0006-291x(73)91228-x
复制
发表时间：
1973-01-01
影响因子：
3.1
通讯作者：
RIBBONS, DW
中科院分区：
文献类型：
--
作者：
GROSECLOSE, EE;RIBBONS, DW
Abstract An inducible 3-hydroxybenzoate 6-hydroxylase has been purified to homogeneity from Pseudomonas aeruginosa. It contains FAD as a prosthetic group. 3-Hydroxybenzoate is quantitatively hydroxylated to give gentisate with equimolar consumptions of NADH and O 2. NADPH will substitute as an electron donor, and several aromatic analogues of 3-hydroxybenzoate stimulate reduced nucleotide oxidation by the enzyme with formation of both hydrogen peroxide and hydroxylated products. Of various analogues of 3-hydroxybenzoate, those substituted in 2, 4, 5 and 6-positions are competent substrates; partial uncoupling of electron flow from hydroxylation with concomitant formation of hydrogen peroxide and “gentisates” occurs. The “natural” product of the reaction, gentisate, is an effector in that it stimulates NADH oxidation with the formation of hydrogen peroxide. 3-hydroxybenzoate 6-hydroxylase thus resembles other flavoprotein hydroxylases in the general regulatory properties dictated by their aromatic substrates, pseudosubstrates or effectors.
