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

Friedrich, T; Strohdeicher, M; Hofhaus, G; Preis, D; Sahm, H; Weiss, H

Friedrich, T; Strohdeicher, M; Hofhaus, G; Preis, D; Sahm, H; Weiss, H.

Affiliation

Friedrich T; Institut für Biochemie, Universität Düsseldorf, FRG.

FEBS Lett ; 265(1-2): 37-40, 1990 Jun 04.

Article in En | MEDLINE | ID: mdl-2142103

Subject(s)

Bacteria/enzymology; Carbohydrate Dehydrogenases/genetics; Chloroplasts/enzymology; Cytochrome Reductases/genetics; Glucose Dehydrogenases/genetics; Mitochondria/enzymology; NADH Dehydrogenase/genetics; Ubiquinone/metabolism; Amino Acid Sequence; Bacteria/genetics; Chlamydomonas/enzymology; Chlamydomonas/genetics; Genes; Glucose 1-Dehydrogenase; Humans; Models, Structural; Molecular Sequence Data; Neurospora crassa/enzymology; Neurospora crassa/genetics; Oxidation-Reduction; Protein Conformation; Sequence Homology, Nucleic Acid

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Collection: 01-internacional Database: MEDLINE Main subject: Bacteria / Carbohydrate Dehydrogenases / Chloroplasts / Ubiquinone / Cytochrome Reductases / Glucose Dehydrogenases / Mitochondria / NADH Dehydrogenase Type of study: Prognostic_studies Limits: Humans Language: En Journal: FEBS Lett Year: 1990 Type: Article

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