Membrane-associated NADH dehydrogenase activities in Rhodobacter capsulatus: purification of a dihydrolipoyl dehydrogenase

1 August 1993

journal article
Published by Microbiology Society in Journal of General Microbiology

Vol. 139 (8) , 1841-1851
https://doi.org/10.1099/00221287-139-8-1841

Abstract

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.

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