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Spectroscopic Characterisation of the Naphthalene Dioxygenase from Rhodococcus sp. Strain NCIMB12038

1
Department of Biotechnology, Chemistry and Pharmacy, Via A. Moro 2, 53100 Siena, Italy
2
Consorzio per lo Sviluppo dei Sistemi a Grande Interfase (CSGI), via della Lastruccia 3, 50019 Sesto Fiorentino, Italy
3
School of Biological Sciences, Queen’s University Belfast, 19 Chlorine Gardens, Belfast BT9 5DL, UK
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(14), 3402; https://doi.org/10.3390/ijms20143402
Received: 31 May 2019 / Revised: 1 July 2019 / Accepted: 9 July 2019 / Published: 11 July 2019
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Abstract

Polycyclic aromatic hydrocarbons (PAHs), such as naphthalene, are potential health risks due to their carcinogenic and mutagenic effects. Bacteria from the genus Rhodococcus are able to metabolise a wide variety of pollutants such as alkanes, aromatic compounds and halogenated hydrocarbons. A naphthalene dioxygenase from Rhodococcus sp. strain NCIMB12038 has been characterised for the first time, using electron paramagnetic resonance (EPR) spectroscopy and UV-Vis spectrophotometry. In the native state, the EPR spectrum of naphthalene 1,2-dioxygenase (NDO) is formed of the mononuclear high spin Fe(III) state contribution and the oxidised Rieske cluster is not visible as EPR-silent. In the presence of the reducing agent dithionite a signal derived from the reduction of the [2Fe-2S] unit is visible. The oxidation of the reduced NDO in the presence of O2-saturated naphthalene increased the intensity of the mononuclear contribution. A study of the “peroxide shunt”, an alternative mechanism for the oxidation of substrate in the presence of H2O2, showed catalysis via the oxidation of mononuclear centre while the Rieske-type cluster is not involved in the process. Therefore, the ability of these enzymes to degrade recalcitrant aromatic compounds makes them suitable for bioremediative applications and synthetic purposes. View Full-Text
Keywords: naphthalene dioxygenase; rieske-type cluster; electron paramagnetic resonance (EPR); spin state; peroxide shunt naphthalene dioxygenase; rieske-type cluster; electron paramagnetic resonance (EPR); spin state; peroxide shunt
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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MDPI and ACS Style

Baratto, M.C.; Lipscomb, D.A.; Larkin, M.J.; Basosi, R.; Allen, C.C.R.; Pogni, R. Spectroscopic Characterisation of the Naphthalene Dioxygenase from Rhodococcus sp. Strain NCIMB12038. Int. J. Mol. Sci. 2019, 20, 3402.

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