The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase

FEBS Letters

Strohdeicher, Michael²  Preis, Dagmar¹  Weiss, Hanns¹  Sahm, Hermann²  Hofhaus, Götz¹  Friedrich, Thorsten¹ 

[1] Institut für Biochemie, Universität Düsseldorf, Universitätsstraße 1, 4000 Düsseldorf 2, FRG;Institut für Biotechnologie, Forschungsanlage Jülich GmbH, Postfach 2050, 5170 Jülich 1, FRG

关键词: NADH dehydrogenase;    Glucose dehydrogenase;    Ubiquinone;    Piericidin;    Proton translocation;    DNA;    mitochondrial;   

DOI  :  10.1016/0014-5793(90)80878-M

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown