Cyanobacteria contain a mitochrondrial complex I‐homologous NADH‐dehydrogenase

FEBS Letters

Ellersiek, Ulrike¹  Steinmüller, Klaus¹  Berger, Susanne¹ 

[1] Institut für Entwicklungs- und Molekularbiologie der Pflanzen, Heinrich-Heine-Universität Düsseldorf, UniversitätsstrasBe 1, D-4000 Düsseldorf 1, Germany

关键词: Respiratory chain;    NADH-dehydrogenase;    Cyanobacteria;    psbG/ndhK;    ndhJ;    Synechocystis 6803;   

DOI  :  10.1016/0014-5793(91)80957-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown