TAILIEUCHUNG - báo cáo khoa hoc : Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L.

Cationic cell wall-bound peroxidase (CWPO-C) has the capability to oxi-dize sinapyl alcohol, ferrocytochromec, and synthetic lignin polymers, unlike most peroxidases that have been characterized in flowering plants, such as horseradish peroxidase and Arabidopsis thalianaperoxidase A2. | IFEBS Journal Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L. Jun Shigeto Yoshitaka Itoh Yuji Tsutsumi and Ryuichiro Kondo Department of Forest and Forest Products Sciences Kyushu University Fukuoka Japan Keywords electron transfer lignification plant peroxidase Populus alba L. protein engineering Correspondence Y. Tsutsumi Department of Forest and Forest Products Sciences Kyushu University 6-10-1 Hakozaki Higashi-ku Fukuoka 812-8581 Japan Fax 81 92 642 4282 Tel 81 92 642 4282 E-mail y-tsutsu@ Received 22 July 2011 revised 9 November 2011 accepted 10 November 2011 doi Cationic cell wall-bound peroxidase CWPO-C has the capability to oxidize sinapyl alcohol ferrocytochrome c and synthetic lignin polymers unlike most peroxidases that have been characterized in flowering plants such as horseradish peroxidase and Arabidopsis thaliana peroxidase A2. It has been suggested that the oxidation site is located on the CWPO-C surface and homology modeling and chemically modified CWPO-C studies suggest that Tyr74 and or Tyr177 are possible participants in the catalytic site. The present study clarifies the importance of these Tyr residues for substrate oxidation using recombinant CWPO-C and recombinant mutant CWPO-C with phenylalanine substitution s for tyrosine. Such recombinant proteins produced in Escherichia coli as inclusion bodies were successfully refolded to yield the active form and purified recombinant protein solutions exhibited typical spectra of high-spin ferric protein and displayed H2O2-dependent oxidation of guaiacol 2 6-dimethoxyphenol and syring-aldazine. Measurement of peroxidase activity with these guaiacyl and syringyl compounds as reducing substrates indicated that a single mutation Y74F or Y177F resulted in substantial loss of oxidation activity 4060 and 82 respectively . Also over 95 of the oxidation activity was lost with a .

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