期刊
BIOPHYSICAL JOURNAL
卷 94, 期 6, 页码 2434-2441出版社
CELL PRESS
DOI: 10.1529/biophysj.107.122614
关键词
-
类别
A comprehensive study of the thermodynamic redox behavior of the berries of the ba(3) enzyme from Thermus thermophilus, a B-type heme-copper oxygen reductase, is presented. This enzyme, in contrast to those having a single type of heme, allows the B- and A-type hemes to be monitored separately by visible spectroscopy and the reduction potential of each heme to be determined unequivocally. The relative order of the midpoint reduction potentials of each center changed in the pH range from 6 to 8.4, and both hemes present a significant redox-Bohr effect. For instance, at pH 7, the midpoint reduction potentials of the hemes B and A(3) are 213 mV and 285 mV, respectively, whereas at pH 8.4, the order is reversed: 246 mV for heme B and 199 mV for heme A(3). The existence of redox anti coope rativity was established by introducing a redox interaction parameter in a model of pairwise interacting redox centers.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据