Journal
BIOELECTROCHEMISTRY
Volume 77, Issue 2, Pages 82-88Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.bioelechem.2009.06.013
Keywords
Collagen; Copper-containing nitrite reductase; Electrocatalytic reduction of nitrite; NO; Model complex
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The electrocatalytic reduction of nitrite to NO by CuMe(2)bpaCl(2), which is a model for the active site of copper-containing nitrite reductase, incorporated into collagen film was investigated. The 77-K EPR spectrum of CuMe(2)bpaCl(2) in the collagen matrix revealed the typical axial signals (g(//)=2.26, g(perpendicular to)=2.05, A(//)=16.4mT) of a tetragonal Cu2+ chromophore. The redox potential, which is related to the Cu+/Cu2+ couple, was -63 mV (Delta E= 72 mV) at pH 5.5. In the presence of nitrite, an increase in the cathodic current was observed in the cyclic voltammogram of CuMe(2)bpaCl(2) in the collagen matrix. Upon reaching - 300 mV, a linear generation of NO was observed for the CuMe(2)bpaCl(2)/collagen film-coated electrode. The relationship between the rate of NO generation and the nitrite concentration in solution was analyzed using the Michaelis-Menten equation, where V-max = 3.16 nM s(-1) and K-m = 1.1 mM at pH 5.5. The current increase and the reaction rate were dependent on the pH of the solution. The mechanism of nitrite reduction by the copper complex in the collagen matrix was the same mechanism as that of the enzyme in aqueous solution. (c) 2009 Elsevier B.V. All rights reserved.
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