CYANOBACTERIA CONTAIN A MITOCHRONDRIAL COMPLEX-I-HOMOLOGOUS NADH-DEHYDROGENASE

被引：70

作者：

BERGER, S ^{[1
]}

ELLERSIEK, U ^{[1
]}

STEINMULLER, K ^{[1
]}

机构：

[1] UNIV DUSSELDORF, INST ENTWICKLUNGS & MOLEK BIOL PFLANZEN, UNIV STR 1, W-4000 DUSSELDORF 1, GERMANY

来源：

FEBS LETTERS | 1991年 / 286卷 / 1-2期

关键词：

RESPIRATORY CHAIN; NADH-DEHYDROGENASE; CYANOBACTERIA; PSBG NDHK; NDHJ; SYNECHOCYSTIS-6803;

D O I：

10.1016/0014-5793(91)80957-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 beta-D-dodecylmaltoside. Sedimentation analysis of the solubilized enzyme on a sucrose gradient indicates that it is a multisubunit protein complex.

引用

页码：129 / 132

页数：4

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