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The presence of several NADH dehydrogenase activities associated with cytoplasmic membrane vesicles of chemoheterotrophically grown Rhodobacter capsulatus MT1131 was demonstrated by combining isoelectric focusing with NADH-tetranitrobluetetrazolium activity staining, a procedure that should have general applicability in the analysis of bacterial NADH dehydrogenase activities. Low pI (pI = 5.7), Mid pI (pI = 6.9) and High pI (pI = 8.5) bands were resolved. The Mid pI NADH dehydrogenase activity was purified and identified as a dihydrolipoyl dehydrogenase. Our data indicate that this dihydrolipoyl dehydrogenase is derived from a 2-oxoacid dehydrogenase complex which is associated with the cytoplasmic membrane.

Original publication

DOI

10.1099/00221287-139-8-1841

Type

Journal article

Journal

J Gen Microbiol

Publication Date

08/1993

Volume

139

Pages

1841 - 1851

Keywords

Amino Acid Sequence, Cell Membrane, Dihydrolipoamide Dehydrogenase, Electrophoresis, Polyacrylamide Gel, Isoelectric Focusing, Molecular Sequence Data, NADH Dehydrogenase, Rhodobacter capsulatus, Sequence Homology, Amino Acid, Solubility