Ferredoxin-NADP+ oxidoreductase is the respiratory NADPH dehydrogenase of the cyanobacterium Anabaena variabilis

Scherer, Siegfried; Alpes, Irene; Sadowski, Heike; Böger, Peter

doi:10.1016/0003-9861(88)90027-6

Cited by 38 publications

(27 citation statements)

References 34 publications

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“…strain PCC 6803 (8). This result is consistent with earlier observations that suggested that respiratory electron transport chains occurred on both under conditions which favor cyclic electron flow (1,38,39,45,46).…”

supporting

confidence: 92%

Isolation and characterization of the ndhF gene of Synechococcus sp. strain PCC 7002 and initial characterization of an interposon mutant

1993

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The ndhF gene of the unicellular marine cyanobacterium Synechococcus sp. strain PCC 7002 was cloned and characterized. NdhF is a subunit of the type 1, multisubunit NADH:plastoquinone oxidoreductase (NADH dehydrogenase). The nucleotide sequence of the gene predicts an extremely hydrophobic protein of 664 amino acids with a calculated mass of 72.9 kDa. The ndhF gene was shown to be single copy and transcribed into a monocistronic mRNA of 2,300 nucleotides. An ndhF null mutation was successfully constructed by interposon mutagenesis, demonstrating that NdhF is not required for cell viability under photoautotrophic growth conditions. The mutant strain exhibited a negligible rate of oxygen uptake in the dark, but its photosynthetic properties (oxygen evolution, chlorophyll/P700 ratio, and chlorophyll/P680 ratio) were generally similar to those of the wild type. Although the ndhF mutant strain grew as rapidly as the wild-type strain at high light intensity, the mutant grew more slowly than the wild type at lower light intensities and did not grow at all under photoheterotrophic conditions. The roles of the NADH:plastoquinone oxidoreductase in photosynthetic and respiratory electron transport are discussed.During respiration in mitochondria, NADH is oxidized and electrons are passed through a series of membranebound oxidoreductase complexes to oxygen. These enzymes combine electron transfer reactions to the vectoral translocation of protons across the inner mitochondrial membrane, thereby generating a proton motive force which can be used for ATP synthesis or other energy-requiring processes (55). The first major enzyme complex (complex I) in this chain is NADH:ubiquinone oxidoreductase (EC 1.6.99.3, also referred to as NADH dehydrogenase; for recent reviews, see references 16, 53, and 55). This mitochondrial enzyme comprises more than 40 subunits, and recently the primary structures of all known components of the bovine complex have been determined (2,4,5,16,53,54). Although some of these subunits are encoded in the mitochondrial genome, the majority of them are encoded in the nucleus and must be imported into the mitochondria and assembled in the inner membrane (16,53,55).A surprising finding from analyses of the complete nucleotide sequences of the chloroplast genomes of liverwort (40), tobacco (48), and rice (23) is that these genomes contain 11 genes with sequence similarity to components of the mitochondrial NADH dehydrogenase. Although it is known that these genes are transcribed (29), the protein products of the chloroplast ndh genes and the putative NADH dehydrogenase which they would form have not yet been identified. Sporadic reports concerning the occurrence of a respiratory chain in the chloroplasts of algae and higher plants have appeared (7,21,31,41); however, the role of such an electron transport chain in chloroplast function is not well understood at present.Several procaryotes have been shown to possess two types of NADH dehydrogenases, only one of which is coupled to proton translocation (60). The ...

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confidence: 92%

Isolation and characterization of the ndhF gene of Synechococcus sp. strain PCC 7002 and initial characterization of an interposon mutant

1993

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“…Similarly to PQ in thylakoid membranes, ubiquinone functions as a mobile electron carrier in respiratory electron transport chains located in the plasma membrane of most aerobic bacteria and in the inner mitochondrial membranes of eukaryotes. Cyanobacteria, however, possess respiratory electron transport chains in both the plasma and the thylakoid membrane but do not synthesize ubiquinone (1)(2)(3). Rather, PQ seems to be the only diffusible prenylquinone in cyanobacterial electron transfer pathways.…”

Section: Plastoquinone (Pq)mentioning

confidence: 99%

Chorismate Pyruvate-Lyase and 4-Hydroxy-3-solanesylbenzoate Decarboxylase Are Required for Plastoquinone Biosynthesis in the Cyanobacterium Synechocystis sp. PCC6803

Pfaff

Glindemann

Gruber

et al. 2014

Journal of Biological Chemistry

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Background: Plastoquinone biosynthesis in cyanobacteria differs from that in plants.Results: Chorismate pyruvate-lyase and 4-hydroxy-3-solanesylbenzoate decarboxylase single-gene knock-out mutants are severely affected in plastoquinone synthesis, cell size/structure, and growth. Conclusion: The plastoquinone biosynthetic pathway likely evolved from a pre-existing ubiquinone pathway in cyanobacterial ancestors. Significance: Cyanobacterial mutants deficient in plastoquinone biosynthesis allow deeper understanding of processes related to energy transformation.

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“…In nonphotosynthetic root plastids a genetically distinct FNR isoform is postulated to function in the opposite direction, providing electrons for nitrogen assimilation at the expense of NADPH generated by heterotrophic metabolism (1,2). It has been suggested, for both cyanobacteria and plastids, that FNR could participate in respiration and cyclic electron transfer as an NADPH dehydrogenase (3)(4)(5)(6).…”

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confidence: 99%

A second isoform of the ferredoxin:NADP oxidoreductase generated by an in-frame initiation of translation

Thomas

Ughy

Lagoutte

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

100

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Ferredoxin:NADP oxidoreductases (FNRs) constitute a family of flavoenzymes that catalyze the exchange of reducing equivalents between one-electron carriers and the two-electron-carrying NADP(H). The main role of FNRs in cyanobacteria and leaf plastids is to provide the NADPH for photoautotrophic metabolism. In root plastids, a distinct FNR isoform is found that has been postulated to function in the opposite direction, providing electrons for nitrogen assimilation at the expense of NADPH generated by heterotrophic metabolism. A multiple gene family encodes FNR isoenzymes in plants, whereas there is only one FNR gene (petH) in cyanobacteria. Nevertheless, we detected two FNR isoforms in the cyanobacterium Synechocystis sp. strain PCC6803. One of them (FNR S Ϸ34 kDa) is similar in size to the plastid FNR and specifically accumulates under heterotrophic conditions, whereas the other one (FNRL Ϸ46 kDa) contains an extra N-terminal domain that allows its association with the phycobilisome. Site-directed mutants allowed us to conclude that the smaller isoform, FNR S, is produced from an internal ribosome entry site within the petH ORF. Thus we have uncovered a mechanism by which two isoforms are produced from a single gene, which is, to our knowledge, novel in photosynthetic bacteria. Our results strongly suggest that FNRL is an NADP ؉ reductase, whereas FNRS is an NADPH oxidase.

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Ferredoxin-NADP+ oxidoreductase is the respiratory NADPH dehydrogenase of the cyanobacterium Anabaena variabilis

Cited by 38 publications

References 34 publications

Isolation and characterization of the ndhF gene of Synechococcus sp. strain PCC 7002 and initial characterization of an interposon mutant

Isolation and characterization of the ndhF gene of Synechococcus sp. strain PCC 7002 and initial characterization of an interposon mutant

Chorismate Pyruvate-Lyase and 4-Hydroxy-3-solanesylbenzoate Decarboxylase Are Required for Plastoquinone Biosynthesis in the Cyanobacterium Synechocystis sp. PCC6803

A second isoform of the ferredoxin:NADP oxidoreductase generated by an in-frame initiation of translation

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