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The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase
Author(s) -
Friedrich Thorsten,
Strohdeicher Michael,
Hofhaus Götz,
Preis Dagmar,
Sahm Hermann,
Weiss Hanns
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80878-m
Subject(s) - nadh dehydrogenase , respiratory chain , dehydrogenase , biochemistry , oxidoreductase , redox , branched chain alpha keto acid dehydrogenase complex , enzyme , electron transport chain , chemistry , mitochondrion , succinate dehydrogenase , submitochondrial particle , biology , protein subunit , organic chemistry , gene
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.