@article {2369,
	title = {Copper-containing nitrite reductase from Pseudomonas chlororaphis DSM 50135 - Evidence for modulation of the rate of intramolecular electron transfer through nitrite binding to the type 2 copper center},
	journal = {European Journal of Biochemistry},
	volume = {271},
	number = {12},
	year = {2004},
	note = {<p>Times Cited: 13</p>
},
	month = {Jun},
	pages = {2361-2369},
	abstract = {<p>The nitrite reductase (Nir) isolated from Pseudomonas chlororaphis DSM 50135 is a blue enzyme, with type 1 and type 2 copper centers, as in all copper-containing Nirs described so far. For the first time, a direct determination of the reduction potentials of both copper centers in a Cu-Nir was performed: type 2 copper (T2Cu), 172 mV and type 1 copper (T1Cu), 298 mV at pH 7.6. Although the obtained values seem to be inconsistent with the established electron-transfer mechanism, EPR data indicate that the binding of nitrite to the T2Cu center increases its potential, favoring the electron-transfer process. Analysis of the EPR spectrum of the turnover form of the enzyme also suggests that the electron-transfer process between T1Cu and T2Cu is the fastest of the three redox processes involved in the catalysis: (a) reduction of T1Cu; (b) oxidation of T1Cu by T2Cu; and (c) reoxidation of T2Cu by NO2-. Electrochemical experiments show that azurin from the same organism can donate electrons to this enzyme.</p>
},
	isbn = {0014-2956},
	url = {http://dx.doi.org/10.1111/j.1432-1033.2004.04155.x},
	author = {Pinho, D. and Besson, S. and Brondino, C. D. and de Castro, B. and Moura, I.}
}
