THE SAME DOMAIN MOTIF FOR UBIQUINONE REDUCTION IN MITOCHONDRIAL OR CHLOROPLAST NADH DEHYDROGENASE AND BACTERIAL GLUCOSE-DEHYDROGENASE

被引：66

作者：

FRIEDRICH, T ^{[1
]}

STROHDEICHER, M ^{[1
]}

HOFHAUS, G ^{[1
]}

PREIS, D ^{[1
]}

SAHM, H ^{[1
]}

WEISS, H ^{[1
]}

机构：

[1] FORSCH ANLAGE GMBH, INST BIOTECHNOL, W-5170 JULICH 1, GERMANY

来源：

FEBS LETTERS | 1990年 / 265卷 / 1-2期

关键词：

DNA; mitochondrial; Glucose dehydrogenase; NADH dehydrogenase; Piericidin; Proton translocation; Ubiquinone;

D O I：

10.1016/0014-5793(90)80878-M

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：

The respiratory chain NADH:ubiquinone oxidoreductase (NADH dehydrogenase or Complex I) of mitochondria comprises some 30 different subunits, and one FMN and 4 or 5 iron-sulfur clusters as internal redox groups. The bacterial glucose dehydrogenase, which oxidizes glucose to gluconolactone in the periplasmatic space and transfers the electrons to ubiquinone, is a single polypeptide chain with pyrolloquinoline quinone as the only redox group. We report here that the two different enzymes have the same ubiquinone binding domain motif and we discuss the predicted membrane folding of this domain with regard to its role in the proton translocating function of the two enzymes. © 1990.

引用

页码：37 / 40

页数：4

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