Characterisation of [Cu4S], the catalytic site in nitrous oxide reductase, by EPR spectroscopy

Dalton Transactions : an International Journal of Inorganic Chemistry
Vasily S OganesyanA J Thomson

Abstract

The enzyme nitrous oxide reductase (N(2)OR) has a unique tetranuclear copper centre [Cu(4)S], called Cu(Z), at the catalytic site for the two-electron reduction of N(2)O to N(2). The X- and Q-band EPR spectra have been recorded from two forms of the catalytic site of the enzyme N(2)OR from Paracoccus pantotrophus, namely, a form prepared anaerobically, Cu(Z), that undergoes a one-electron redox cycle and Cu(Z)*, prepared aerobically, which cannot be redox cycled. The spectra of both species are axial with that of Cu(Z) showing a rich hyperfine splitting in the g||-region at X-band. DFT calculations were performed to gain insight into the electronic configuration and ground-state properties of Cu(Z) and to calculate EPR parameters. The results for the oxidation state [Cu(+1)(3)Cu(+2)(1)S](3+) are in good agreement with values obtained from the fitting of experimental spectra, confirming the absolute oxidation state of Cu(Z). The unpaired spin density in this configuration is delocalised over four copper ions, thus, Cu(I) 20.1%, Cu(II) 9.5%, Cu(III) 4.8% and Cu(IV) 9.2%, the mu(4)-sulfide ion and oxygen ligand. The three copper ions carrying the highest spin density plus the sulfide ion lie approximately in the same plane while t...Continue Reading

Citations

Feb 12, 2009·Journal of the American Chemical Society·Itsik Bar-NahumWilliam B Tolman
Mar 28, 2012·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Simone Dell'AcquaIsabel Moura
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Dec 9, 2017·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Peter M H Kroneck
Oct 20, 2005·Dalton Transactions : an International Journal of Inorganic Chemistry·Tim RasmussenAndrew J Thomson
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Sep 21, 2017·Journal of Inorganic Biochemistry·Cíntia CarreiraIsabel Moura
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