Ferrodoxin and flavodoxin from the cyanobacterium Synechocystis sp PCC 6803

Bottin, Hervé; Lagoutte, Bernard

doi:10.1016/0167-4838(92)90465-p

Cited by 121 publications

(86 citation statements)

References 32 publications

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“…The isoelectric point was determined to be 3.6. As has been shown to occur with highly acidic proteins [39] the value obtained may be overestimated, although there is an excellent agreement between both molecular mass determinations. The iron quantification gave a value of 7 ?…”

Section: Methodsmentioning

confidence: 54%

A Seven‐iron Ferredoxin from the Thermoacidophilic Archaeon Desulfurolobus ambivalens

Teixeira

Batista

Campos

et al. 1995

European Journal of Biochemistry

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A seven-iron ferredoxin was isolated from aerobically grown cells of the hyperthermoacidophilic archaleon Desulfurolobus ambivalens (DSM 3772). The protein is monomeric, with an apparent molecular mass of 15 kDa and contains 7 iron atoms/molecule. The N-terminal sequence shows a large similarity (70% identity) with that of the ferredoxin isolated from the archaeon Sulfolobus acidocaldarius. The EPR isharacteristics in both the native (oxidized) and dithionite-reduced states of this protein allowed an unequivocal identification of a [3Fe-4SI1+" center, with a reduction potential of -270-+ 20 mV, at pH 7.5. The protein also contains a [4Fe-4S]*'"+ center with a very low reduction potential (Eo = -540 mV, pH 7.1D), which yields a rhombic EPR spectrum upon reduction with sodium dithionite at high pH. The reduction potentials of both centers are slightly pH dependent between pH 6 and 9. The [3Fe-4S] ferredoxin center is able to accept electrons from pyruvate oxidase and NADH oxidase isolated from D. ambivalens. This ferredoxin is present in large amounts (at least 130 mgkg wet cells), which allowed the unequivocal observation of oxidized [3Fe-4S] clusters in intact D. ambivalens cells.Keywords. Iron-sulfur centers ; Archaea; EPR; thermophilic.Proteins containing iron-sulfur clusters with a wide range of stoichiometries are ubiquitously found to be involved in fundamental biological processes like nitrogen fixation, CO, fixation, hydrogen metabolism, the citric-acid cycle, detoxification and membrane-bound (energy-transduction processes [l -31. The simplest iron-sulfur proteins, the ferredoxins, are involved in these pathways as one-electron carriers. Due mainly to the extensive work on model compounds, it has been shown that under anaerobic conditions iron-sulfur structures may self-assemble in reaction mixtures containing iron, sulfide and thiols [4]. Thus, since iron-sulfur proteins are present in the three major urkingdoms, they were proposed as the most ancient electron-transfer agents to have appeared during biological evolution [5]. Therefore, in evolutionary terms it is particularly interesting to screen ffor iron-sulfur proteins in archaea, the most ancient living organisms [6].

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Section: Methodsmentioning

confidence: 54%

A Seven‐iron Ferredoxin from the Thermoacidophilic Archaeon Desulfurolobus ambivalens

Teixeira

Batista

Campos

et al. 1995

European Journal of Biochemistry

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“…This ferredoxin contains a 2Fe-2S cluster, and its retention authenticates the anaerobic nature of these analyses. Moreover, when iron supply is limiting, Synechocystis PCC 6803 replaces ferredoxin with flavodoxin (37). Thus, there is dual reciprocal switching in this system, from plastocyanin in low copper and from ferredoxin in low iron.…”

Section: Discussionmentioning

confidence: 99%

A Periplasmic Iron-binding Protein Contributes toward Inward Copper Supply

Waldron¹,

Tottey²,

Yanagisawa

et al. 2007

Journal of Biological Chemistry

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Periplasmic substrate binding proteins are known for iron, zinc, manganese, nickel, and molybdenum but not copper. Synechocystis PCC 6803 requires copper for thylakoid-localized plastocyanin and cytochrome oxidase. Here we show that mutants deficient in a periplasmic substrate binding protein FutA2 have low cytochrome oxidase activity and produce cytochrome c 6 when grown under copper conditions (150 nM) in which wild-type cells use plastocyanin rather than cytochrome c 6 . Anaerobic separation of extracts by two-dimensional native liquid chromatography followed by metal analysis and peptide mass-fingerprinting establish that accumulation of copperplastocyanin is impaired, but iron-ferredoxin is unaffected in ⌬futA2 grown in 150 nM copper. However, recombinant FutA2 binds iron in preference to copper in vitro with an apparent Fe(III) affinity similar to that of its paralog FutA1, the principal substrate binding protein for iron import. FutA2 is also associated with iron and not copper in periplasm extracts, and this Fe(III)-protein complex is absent in ⌬futA2. There are differences in the soluble protein and small-molecule complexes of copper and iron, and the total amount of both elements increases in periplasm extracts of ⌬futA2 relative to wild type. Changes in periplasm protein and small-molecule complexes for other metals are also observed in ⌬futA2. It is proposed that FutA2 contributes to metal partitioning in the periplasm by sequestering Fe(III), which limits aberrant Fe(III) associations with vital binding sites for other metals, including copper.Oxygenic phototrophs have exceptional requirements for metals such as iron, copper, and manganese within the photosynthetic machinery (1, 2). There is interest in understanding how metal ions partition to the correct cellular destinations in all organisms (3), including to the approximately one-third of proteins that need metals (4). The periplasm is a key location for metal partitioning. Bacterial ATP binding cassette (ABC)-type importers include substrate binding proteins which may be free within the periplasm or anchored to the outer face of the plasma membrane. It is anticipated that these proteins assist in loading metal ions onto the correct importers. There is similarity in the metal-binding sites of several substrate binding proteins that contribute toward the import of distinct metals, such as manganese versus zinc, and subtle differences in second coordination spheres may be crucial for metal selectivity (5). It has also been noted that the nature of interactions between substrate binding proteins and their respective metal transporters may make a key contribution to metal specificity (5

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“…Ferredoxin from Svnechocvstis 6803 was isolated and purified according to Bottin and Lagoutte (1992). PSI from Svnechocvstis 6803 was isolated as described by Rogner et al (1990) and Kruip et al (1993).…”

Section: Biological Materials and Chemical Cross-linkingmentioning

confidence: 99%

Characterization of a redox active cross-linked complex between cyanobacterial photosystem I and soluble ferredoxin.

et al. 1996

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A covalent stoichiometric complex between photosystem I (PSI) and ferredoxin from the cyanobacterium Synechocystis sp. PCC 6803 was generated by chemical cross‐linking. The photoreduction of ferredoxin, studied by laser flash absorption spectroscopy between 460 and 600 nm, is a fast process in 60% of the covalent complexes, which exhibit spectral and kinetic properties very similar to those observed with the free partners. Two major phases with t(1/2) <1 micros and approximately 10–14 micros are observed at two different pH values (5.8 and 8.0). The remaining complexes do not undergo fast ferredoxin reduction and 20–25% of the complexes are still able to reduce free ferredoxin or flavodoxin efficiently, thus indicating that ferredoxin is not bound properly in this proportion of covalent complexes. The docking site of ferredoxin on PSI was determined by electron microscopy in combination with image analysis. Ferredoxin binds to the cytoplasmic side of PSI, with its mass center 77 angstroms distant from the center of the trimer and in close contact with a ridge formed by the subunits PsaC, PsaD and PsaE. This docking site corresponds to a close proximity between the [2Fe‐ 2S] center of ferredoxin and the terminal [4Fe‐4S] acceptor FII of PSI and is very similar in position to the docking site of flavodoxin, an alternative electron acceptor of PSI.

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Ferrodoxin and flavodoxin from the cyanobacterium Synechocystis sp PCC 6803

Cited by 121 publications

References 32 publications

A Seven‐iron Ferredoxin from the Thermoacidophilic Archaeon Desulfurolobus ambivalens

A Seven‐iron Ferredoxin from the Thermoacidophilic Archaeon Desulfurolobus ambivalens

A Periplasmic Iron-binding Protein Contributes toward Inward Copper Supply

Characterization of a redox active cross-linked complex between cyanobacterial photosystem I and soluble ferredoxin.

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