Aniline hydroxylase activities of haemoglobin: Kinetics and mechanism |
| |
Authors: | Bernard Cambou Didier Guillochon Daniel Thomas |
| |
Affiliation: | Laboratoire de Technologie Enzymatique, ERA no. 338 du CNRS, Université de Technologie de Compiègne, B.P. 233, 60206 Compiègne cedex, France |
| |
Abstract: | The mechanism of the aniline hydroxylase activity of methaemoglobin in a monooxygenase system consisting of NADH as electron donor, riboflavin, FAD, FMN or methylene blue as electron carrier and methaemoglobin as the terminal oxidase has been studied. Hydrogen peroxide is produced from oxygen in a methaemoglobin-independent process. 4-Aminophenol is subsequently produced peroxidatively by an NADH-dependent process; NADH prevents a further oxidation of 4-aminophenol in the presence of haemoglobin. In the absence of electron carrier, NADH slowly reduces haemoglobin and then oxyhaemoglobin reacts with aniline to give 4-aminophenol. In the absence of electron donor and electron carrier, oxyhaemoglobin and aniline give rise to the reversible production of 4-aminophenol. |
| |
Keywords: | Haemoglobin methaemoglobin hydroxylation aniline immobilization NADH nicotinamide adenine dinucleotide, reduced form nicotinamide adenine dinucleotide, oxidized form FAD flavin adenine dinucleotide FMN flavin mononucleotide |
本文献已被 ScienceDirect 等数据库收录! |
|