Citation:

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, Pinho, D., Besson S., Brondino C. D., de Castro B., and Moura I. , European Journal of Biochemistry, Jun, Volume 271, Number 12, p.2361-2369, (2004)

Abstract:

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.

Notes:

Times Cited: 13

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