Effects induced by rotenone during aerobic growth ofParacoccus denitrificans in continuous culture

Meijer, E. M.; Schuitenmaker, M. G.; Boogerd, Fred C.; Wever, R.; Stouthamer, A. H.

doi:10.1007/bf00964262

Cited by 31 publications

(19 citation statements)

References 44 publications

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“…Since H+/O ratios are not significantly affected, it is not likely that electron transport is blocked at phosphorylation site I, which is situated between NADH and ubiquinone (25). Rotenone, which is known to inhibit electron transport at this site, reduces the H+/O ratio by about 50% (17). Therefore, the site of inhibition is probably located between ubiquinone and cytochrome b.…”

Section: Discussionmentioning

confidence: 99%

Mode of action of copper complexes of some 2,2'-bipyridyl analogs on Paracoccus denitrificans

Smit¹,

Goot²,

Nauta³

et al. 1980

Antimicrob Agents Chemother

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Copper complexes of 2,2'-bipyridyl and related compounds and CuSO4 inhibited the growth of paracoccus denitrificans. The copper(I) complex of 2,9-dimethyl-1,10-phenanthroline [Cu(DMP)2NO3] showed the highest activity, whereas the copper(II) complex of 1,10-phenanthroline and CuSO4 inhibited the growth to a lesser extent. The uncomplexed ligands (1,10-phenanthroline and 2,9-dimethyl-1,10-phenanthroline) showed little activity, but in the presence of noninhibitory amounts of CuSO4 this activity increased markedly. Copper ions therefore proved to be essential for the growth-inhibitor effect. The extent of inhibition appeared to be strongly dependent on the initial cell density and on the growth medium. No selective inhibition of deoxyribonucleic acid, ribonucleic acid, or protein synthesis was observed with Cu(DMP)2NO3. Respiratory electron transport of P. denitrificans appeared to be strongly inhibited by Cu(DMP)2NO3 and to a somewhat lesser extent by CuSO4. Both aerobic and anaerobic respirations were inhibited to the same extent, and from the cytochrome redox kinetics it is concluded that the site of this inhibition in the respiratory electron transport chain must be located before cytochrome b. Cu(DMP)2NO3 did not significantly influence the H+/O ratio with whole cells of P. denitrificans, suggesting that the efficiency of oxidative phosphorylation is not affected by CU(DMP)2NO3. Growing cultures of P. denitrificans showed a decrease in intracellular potassium ion content in the presence of increasing amounts of Cu(DMP)2NO3. It is concluded that interference with the cytoplasmic membrane, resulting in inhibition of respiratory electron transport, probably constitutes the main mode of action of copper complexes of 2,2'-bipyridyl analogs on P. denitrificans.

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Section: Discussionmentioning

confidence: 99%

Mode of action of copper complexes of some 2,2'-bipyridyl analogs on Paracoccus denitrificans

Smit¹,

Goot²,

Nauta³

et al. 1980

Antimicrob Agents Chemother

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“…For example, it has been shown that during the exponential growth phase of Neurospora crassa or when the mitochondrial translation apparatus is blocked by chloramphenicol, a small isoform of complex I is formed, which lacks iron-sulphur cluster N-2 [14,35]. Likewise, growth in the presence of rotenone leads to the loss of iron-sulphur cluster N-2 in the enzyme ofParacoccus denitrificans [24].…”

Section: Transcription Analysismentioning

confidence: 99%

Cloning and transcription analysis of the ndh(A-I-G-E) gene cluster and the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803

Ellersiek

Steinmüller

1992

Plant Mol Biol

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The plastid DNA of higher plants contains eleven reading frames that are homologous to subunits of the mitochondrial NADH-ubiquinone oxidoreductase (complex I). The genes are expressed, but a plastid NAD(P)H dehydrogenase has not yet been isolated and the function of the enzyme in plastid metabolism is unknown. Cyanobacteria also contain a NADH dehydrogenase that is homologous to the mitochondrial complex I. The enzyme is sensitive to rotenone and is located on the cytoplasmic and the thylakoid membrane. We report here the sequence of five subunits (ndhA, -I, G, -E and -D) of the NADH dehydrogenase from the unicellular cyanobacterium Synechocystis sp. PCC6803. As in plastid DNA, the genes ndh(A-I-G-E) are clustered and probably constitute an operon. The ndhD gene is associated with a gene encoding an iron-sulphur protein of photosystem I (psaC) as in plastid DNA. In contrast to the situation in plastids, psaC and ndhD are not cotranscribed but transcribed from opposite strands. The deduced amino acid sequence of the cyanobacterial polypeptides is more similar to the corresponding plastid (40-68% identity) than to the corresponding mitochondrial subunits (17-39% identity). Thus, the cyanobacterial NADH-dehydrogenase provides a prokaryotic model system which is more suitable to genetic analysis than the enzyme of plastids.

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“…The functional similarity of P. denitrificans NADH:ubiquinone ox idoreductase (complex I) to the mitochondrial enzyme has been reported (306)(307)(308), but purification of the complex has not been accomplished. Although the bacterium possesses a Class IA cytochrome c oxidase as a major component (309), it certainly also has other terminal oxidases, which show the spectroscopic characteristics of Class IB oxidase (309)(310)(311) or Class lIB oxidase (312).…”

Section: General Remarksmentioning

confidence: 99%

Bacterial Electron Transport Chains

Anraku¹

1988

Annu. Rev. Biochem.

227

103

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Effects induced by rotenone during aerobic growth ofParacoccus denitrificans in continuous culture

Cited by 31 publications

References 44 publications

Mode of action of copper complexes of some 2,2'-bipyridyl analogs on Paracoccus denitrificans

Mode of action of copper complexes of some 2,2'-bipyridyl analogs on Paracoccus denitrificans

Cloning and transcription analysis of the ndh(A-I-G-E) gene cluster and the ndhD gene of the cyanobacterium Synechocystis sp. PCC6803

Bacterial Electron Transport Chains

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