章鱼血蓝蛋白被氮氧化物氧化。

The oxidation of Octopus vulgaris hemocyanin by nitrogen oxides.

作者信息

Salvato B, Giacometti G M, Beltramini M, Zilio F, Giacometti G, Magliozzo R S, Peisach J

机构信息

Department of Biology, University of Padova, Italy.

出版信息

Biochemistry. 1989 Jan 24;28(2):680-4. doi: 10.1021/bi00428a040.

DOI:10.1021/bi00428a040

PMID:2540804

Abstract

The reaction of Octopus vulgaris hemocyanin with nitrite was studied under a variety of conditions in which the green half-met derivative is formed. Analytical evidence shows that the amount of chemically detectable nitrite in various samples of the derivative is not proportional to the cupric copper detected by EPR. The kinetics of oxidation of hemocyanin as a function of protein concentration and pH, in the presence of nitrite and ascorbate, is consistent with a scheme in which NO2 is the reactive oxidant. We suggest that the green half-methemocyanin contains a metal center with one cuprous and one cupric copper without an exogenous nitrogen oxide ligand.

摘要

在多种形成绿色半金属衍生物的条件下，研究了普通章鱼血蓝蛋白与亚硝酸盐的反应。分析证据表明，衍生物不同样品中化学可检测的亚硝酸盐量与通过电子顺磁共振检测到的铜离子不成正比。在亚硝酸盐和抗坏血酸存在的情况下，血蓝蛋白氧化动力学作为蛋白质浓度和pH的函数，与以NO2为活性氧化剂的反应机制一致。我们认为，绿色半金属血蓝蛋白含有一个金属中心，其中有一个亚铜离子和一个铜离子，且没有外源氮氧化物配体。