A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus. Export

@article{citeulike:5753283, abstract = {The amine oxygenase AurF from Streptomyces thioluteus catalyzes the six-electron oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA). In this work, we have studied the reaction of its reduced Fe(2)(II/II) cofactor with O(2), which results in generation of a peroxo-Fe(2)(III/III) intermediate. In the absence of substrate, this intermediate is unusually stable (t(1/2) = 7 min at 20 degrees C), allowing for its accumulation to almost stoichiometric amounts. Its decay is accelerated approximately 10(5)-fold by the substrate, pABA, implying that it is the complex that effects the two-electron oxidation of the amine to the hydroxylamine. The nearly quantitative conversion of pABA to pNBA by solutions containing an excess of the intermediate suggests that it may also be competent for the two subsequent two-electron oxidations leading to the product.}, author = {Korboukh, Victoria Korneeva K. and Li, Ning and Barr, Eric W. and Bollinger, J. Martin and Krebs, Carsten}, citeulike-article-id = {5753283}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/ja9064969}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/ja9064969}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/19731912}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=19731912}, day = {30}, doi = {10.1021/ja9064969}, issn = {1520-5126}, journal = {Journal of the American Chemical Society}, keywords = {aurf, biometal, non, non\_heme\_iron}, month = {September}, number = {38}, pages = {13608--13609}, posted-at = {2009-09-08 22:26:05}, priority = {2}, title = {A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus.}, url = {http://dx.doi.org/10.1021/ja9064969}, volume = {131}, year = {2009} }

TY - JOUR ID - citeulike:5753283 L3 - citeulike-article-id:5753283 N2 - The amine oxygenase AurF from Streptomyces thioluteus catalyzes the six-electron oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA). In this work, we have studied the reaction of its reduced Fe(2)(II/II) cofactor with O(2), which results in generation of a peroxo-Fe(2)(III/III) intermediate. In the absence of substrate, this intermediate is unusually stable (t(1/2) = 7 min at 20 degrees C), allowing for its accumulation to almost stoichiometric amounts. Its decay is accelerated approximately 10(5)-fold by the substrate, pABA, implying that it is the complex that effects the two-electron oxidation of the amine to the hydroxylamine. The nearly quantitative conversion of pABA to pNBA by solutions containing an excess of the intermediate suggests that it may also be competent for the two subsequent two-electron oxidations leading to the product. IS - 38 JF - Journal of the American Chemical Society SN - 1520-5126 EP - 13609 TI - A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus. VL - 131 SP - 13608 KW - aurf KW - biometal KW - non KW - non_heme_iron AU - Korboukh, Victoria Korneeva AU - Li, Ning AU - Barr, Eric AU - Bollinger, Martin AU - Krebs, Carsten PY - 2009/09/30/ UR - http://dx.doi.org/10.1021/ja9064969 ER -