TitleDatePubMed ID
The importance of the benzoic acid carboxylate moiety for substrate recognition by CYP199A4 from Rhodopseudomonas palustris HaA2.2016 Jun26969786
Biotechnological production of caffeic acid by bacterial cytochrome P450 CYP199A2.2012 Sep22729547
The crystal structures of 4-methoxybenzoate bound CYP199A2 and CYP199A4: structural changes on substrate binding and the identification of an anion binding site.2012 Jul 2822695988
Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris.2010 Mar19904564
Regioselective oxidation of indole- and quinolinecarboxylic acids by cytochrome P450 CYP199A2.2010 Feb20112454
Crystal structure of CYP199A2, a para-substituted benzoic acid oxidizing cytochrome P450 from Rhodopseudomonas palustris.2008 Nov 1418762195
Cytochrome P450 enzymes from the metabolically diverse bacterium Rhodopseudomonas palustris.2006 Mar 3116472768
Substrate and solvent isotope effects on the fate of the active oxygen species in substrate-modulated reactions of putidamonooxin.2000 Oct10998052
4-Methoxybenzoate monooxygenase from Pseudomonas putida: isolation, biochemical properties, substrate specificity, and reaction mechanisms of the enzyme components.19883226294
Dioxygen activation by putidamonooxin. The oxygen species formed and released under uncoupling conditions.1981 Dec6277620