Abstract：
:Bacterial multicomponent monooxygenases (BMMs) are members of a wide family of diiron enzymes that use molecular oxygen to hydroxylate a variety of aromatic compounds. The presence of genes encoding for accessory proteins not involved in catalysis and whose role is still elusive, is a common feature of the gene clusters of several BMMs, including phenol hydroxylases and several soluble methane monooxygenases. In this study we have expressed, purified, and partially characterized the accessory component PHK of the phenol hydroxylase from Pseudomonas sp. OX1, a bacterium able to degrade several aromatic compounds. The phenol hydroxylase (ph) gene cluster was expressed in Escherichia coli/JM109 cells in the absence and in the presence of the phk gene. The presence of the phk gene lead to an increase in the hydroxylase activity of whole recombinant cells with phenol. PHK was assessed for its ability to interact with the active hydroxylase complex. Our results show that PHK is neither involved in the catalytic activity of the phenol hydroxylase complex nor required for the assembly of apo-hydroxylase. Our results suggest instead that this component may be responsible for enhancing iron incorporation into the active site of the apo-hydroxylase.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Izzo V,Leo G,Scognamiglio R,Troncone L,Birolo L,Di Donato Adoi
10.1016/j.abb.2010.09.023subject
Has Abstractpub_date
2011-01-01 00:00:00pages
48-59issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(10)00415-7journal_volume
505pub_type
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