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| Content Provider | Springer Nature Link |
|---|---|
| Author | Dell’Acqua, Simone Pauleta, Sofia R. Paes de Sousa, Patrícia M. Monzani, Enrico Casella, Luigi Moura, José J. G. Moura, Isabel |
| Copyright Year | 2010 |
| Abstract | The final step of bacterial denitrification, the two-electron reduction of N2O to N2, is catalyzed by a multi-copper enzyme named nitrous oxide reductase. The catalytic centre of this enzyme is a tetranuclear copper site called CuZ, unique in biological systems. The in vitro reconstruction of the activity requires a slow activation in the presence of the artificial electron donor, reduced methyl viologen, necessary to reduce CuZ from the resting non-active state (1CuII/3CuI) to the fully reduced state (4CuI), in contrast to the turnover cycle, which is very fast. In the present work, the direct reaction of the activated form of Pseudomonas nautica nitrous oxide reductase with stoichiometric amounts of N2O allowed the identification of a new reactive intermediate of the catalytic centre, CuZ°, in the turnover cycle, characterized by an intense absorption band at 680 nm. Moreover, the first mediated electrochemical study of Ps. nautica nitrous oxide reductase with its physiological electron donor, cytochrome c-552, was performed. The intermolecular electron transfer was analysed by cyclic voltammetry, under catalytic conditions, and a second-order rate constant of (5.5 ± 0.9) × 105 M−1 s−1 was determined. Both the reaction of stoichiometric amounts of substrate and the electrochemical studies show that the active CuZ° species, generated in the absence of reductants, can rearrange to the resting non-active CuZ state. In this light, new aspects of the catalytic and activation/inactivation mechanism of the enzyme are discussed. |
| Starting Page | 967 |
| Ending Page | 976 |
| Page Count | 10 |
| File Format | |
| ISSN | 09498257 |
| Journal | JBIC Journal of Biological Inorganic Chemistry |
| Volume Number | 15 |
| Issue Number | 6 |
| e-ISSN | 14321327 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2010-04-27 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Nitrous oxide reductase Catalytic mechanism Denitrification Bioelectrochemistry Biochemistry Microbiology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Biochemistry Inorganic Chemistry |
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