Copper-adenine catalyst for O2 production from H2O2

被引:16
作者
Bruston, F
Vergne, J
Grajcar, L
Drahi, B
Calvayrac, R
Baron, MH
Maurel, MC
机构
[1] Univ Denis Diderot, Lab Membranes Biol, F-75251 Paris 05, France
[2] Inst Jacques Monod, F-75251 Paris, France
[3] CNRS, UPR 1580, Lab Dynam Interact & Reactiv, F-94320 Thiais, France
关键词
copper-adenine complex; catalatic activity; hydrogen peroxide; Raman spectroscopy; polarography;
D O I
10.1006/bbrc.1999.1416
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In solutions of CuCl2 and adenine copper can be bound to adenine. Two Cu(adenine)(2) complexes [Cu(C5H5N5)(2)](2+)/Cu(C5H4N5)(2)] are in equilibrium with free adenine. Copper-adenine complexes present a catalatic activity (e.g., H2O2 disproportionation into O-2 and water) but depending on complex concentration H2O2 also strongly oxidizes the adenine within the complexes. Raman spectroscopy quantifies copper-adenine complex formation and H2O2 consumption; polarography quantifies O-2, production. As for C-40 catalase, optimal catalatic capacities depend on physiological conditions, such as pH and temperature. The comparative analysis of kinetic parameters shows that the! affinity for H2O2 of Cu(adenine)(2) is 37-fold lower than that of C-40 catalase and that the molar activity for O-2 production is 200-fold weaker for Cu(adenine)(2) than for the enzyme. In the 10(-6)-10(-3) RI range, the strong decrease of activity with raising complex concentration is explained by aggregation or stacking, which protects Cu(adenine)(2) entities from H2O2 oxidation, but also decreases O-2 production. (C) 1999 Academic Press.
引用
收藏
页码:672 / 677
页数:6
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