TAILIEUCHUNG - Báo cáo khoa học: The oxygenase component of phenol hydroxylase from Acinetobacter radioresistens S13

Phenol hydroxylase (PH) from Acinetobacter radioresis-tensS13 represents anexampleofmulticomponent aromatic ringmonooxygenase made up of three moieties: a reductase (PHR), an oxygenase (PHO) and a regulative component (PHI). The function of the oxygenase component (PHO), here characterized for the first time, is to bind molecular oxygen and catalyse the mono-hydroxylation of substrates (phenol, and with less efficiency, chloro- andmethyl-phenol and naphthol). | Eur. J. Biochem. 270 2244-2253 2003 FEBS 2003 doi The oxygenase component of phenol hydroxylase from Acinetobacter radioresistens S13 Sara Divari1 Francesca Valetti1 Patrizia Caposio4 Enrica Pessione1 Maria Cavaletto2 Ersilia Griva1 Giorgio Gribaudo4 Gianfranco Gilardi1 3 and Carlo Giunta1 1 Dipartimento di Biologia Animate e dell Uomo Universita di Torino Italy 2Dipartimento di Scienze e Tecnologie Avanzate Universita del Piemonte Orientale Alessandria Italy 3Department of Biological Sciences Imperial College of Science Technology and Medicine London UK 4Dipartimento di Sanita Pubblica e Microbiologia Universita di Torino Italy Phenol hydroxylase PH from Acinetobacter radioresis-tens S13 represents an example of multicomponent aromatic ring monooxygenase made up of three moieties a reductase PHR an oxygenase PHO and a regulative component PHI . The function of the oxygenase component PHO here characterized for the first time is to bind molecular oxygen and catalyse the mono-hydroxylation of substrates phenol and with less efficiency chloro- and methyl-phenol and naphthol . PHO was pLIii Íled from extracss iff A. radio-resistens S13 cells and shown to be a dimer of206 kDa. Each monomer is composed by three subunits a 54 kDa b 38 kDa and c 11 kDa . The gene encoding PHO a named mopN was cloned and sequenced and the corresponding amino acid sequence matched with that of functionally related oxygenases. By structural alignment with the catalytic subunits of methane monooxygenase MMO and alkene monooxygenase we propose that PHO a contains the enzyme active site harbouring a dinuclear iron centre Fe-O-Fe as also suggested by spectral analysis. Conserved hydrophobic amino acids known to define the substrate recognition pocket are also present in the a-subunit. The prevalence of a-helices as studied by CD confirmed the hypothized structural homologies between PHOand MMO. Three parameters optimum ionic strength temperature and pH that

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