TAILIEUCHUNG - Báo cáo khoa học: The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity

The multicopper oxidase from the hyperthermophilic archaeonPyrobacu-lum aerophilum (McoP) was overproduced in Escherichia coliand purified to homogeneity. The enzyme consists of a single kDa subunit, and the combined results of UV–visible, CD, EPR and resonance Raman spectroscopies showed the characteristic features of the multicopper oxidases. Analysis of the McoP sequence allowed its structure to be derived by comparative modeling methods. | The multicopper oxidase from the archaeon Pyrobaculum aerophilum shows nitrous oxide reductase activity Andre T. Fernandes1 Joao M. Damas1 Smilja Todorovic1 Robert Huber2 M. Camilla Baratto3 Rebecca Pogni3 Claudio M. Soares1 and Ligia O. Martins1 1 Institute de Tecnologia Quimica e Biologica Universidade Nova de Lisboa Oeiras Portugal 2 Kommunale Berufsfachschule fur biologisch-technische Assistenten Straubing Germany 3 Department of Chemistry University of Siena Italy Keywords Archaea hyperthermophiles multicopper oxidases nitrous oxide reductase Pyrobaculum aerophilum Correspondence L. O. Martins Instituto de Tecnologia Química e Biológica Universidade Nova de Lisboa Av. da Republica 2781-901 Oeiras Portugal Fax 351 214411277 Tel 351 214469534 E-mail lmartins@ Received 13 April2010 revised 25 May 2010 accepted 28 May 2010 doi The multicopper oxidase from the hyperthermophilic archaeon Pyrobaculum aerophilum McoP was overproduced in Escherichia coli and purified to homogeneity. The enzyme consists of a single kDa subunit and the combined results of UV-visible CD EPR and resonance Raman spectroscopies showed the characteristic features of the multicopper oxidases. Analysis of the McoP sequence allowed its structure to be derived by comparative modeling methods. This model provided a criterion for designing meaningful site-directed mutants of the enzyme. McoP is a hyperthermoactive and thermostable enzyme with an optimum reaction temperature of 85 C a half-life of inactivation of 6 h at 80 C and temperature values at the midpoint from 97 to 112 C. McoP is an efficient metallo-oxidase that catalyzes the oxidation of cuprous and ferrous ions with turnover rate constants of 356 and 128 min-1 respectively at 40 C. It is noteworthy that McoP follows a ping-pong mechanism with three-fold higher catalytic efficiency when using nitrous oxide as electron acceptor than when using dioxygen the typical oxidizing substrate of .

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