Cyanobacteria contain a mitochrondrial complex I‐homologous NADH‐dehydrogenase

Abstract
Thylakoid and cytoplasmic membranes of the cyanobacterium Synechocystis sp. PCC 6803 were purified by sucrose gradient centrifugation. Both membranes oxidize NADH in a rotenone‐sensitive reaction. Antibodies prepared against psbG/ndhK and ndhJ fusion proteins detect the corresponding polypeptides in both membrane preparations. This demonstrates that a NADH‐dehydrogenase, homologous to the mitochondrial NADH‐ubiquinone‐oxidoreductase (complex I of the respiratory chain) is present in cyanobacteria. The NADH‐dehydrogenase can be solubilized with the detergent β‐D‐dodecylmaltoside. Sedimentation analysis of the solubilized enzyme on a sucrose gradient indicates that it is a multisubunit protein complex.

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