Cytochrome c oxidase (Heme aa3) from Paracoccus denitrificans:: Analysis of mutations in putative proton channels of subunit I

被引：116

作者：

Pfitzner, U ^{[1
]}

Odenwald, A ^{[1
]}

Ostermann, T ^{[1
]}

Weingard, L ^{[1
]}

Ludwig, B ^{[1
]}

Richter, OMH ^{[1
]}

机构：

[1] Biozentrum, Inst Biochem, D-60439 Frankfurt, Germany

来源：

JOURNAL OF BIOENERGETICS AND BIOMEMBRANES | 1998年 / 30卷 / 01期

关键词：

terminal oxidase; redox coupling; electrochemical gradient; electron transport; energy transduction; proton translocation; crystal structure; site-directed mutagenesis;

D O I：

10.1023/A:1020515713103

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

One of the challenging features of energy-transducing terminal oxidases, like the aa(3) cytochrome c oxidase of Paracoccus denitrificans, is the translocation of protons across the cytoplasmic membrane, which is coupled to the transfer of electrons to oxygen. As a prerequisite for a more advanced examination of the enzymatic properties, several amino acid residues, selected on the basis of recent three-dimensional structure determinations, were exchanged in subunit I of the Paracoccus enzyme by site-directed mutagenesis. The properties of the mutated oxidases were analyzed by different methods to elucidate whether they are involved in the coupled and coordinated transfer of protons via two different pathways either to the site of oxygen reduction or through the enzyme from the cytoplasm to the periplasmic side.

引用

页码：89 / 97

页数：9

共 42 条

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