The Effect of Sulfite on the ATP Hydrolysis and Synthesis Activity of Membrane-Bound H+-ATP Synthase from Various Species

Bakels, R.H.A.; Vanwalraven, H.S.; Vanwielink, J.E.; Vanderzwetdegraaff, I.; Krenn, Bea E.; Krab, Klaas; Berden, J.A.; Kraayenhof, Ruud

doi:10.1006/bbrc.1994.1728

Cited by 19 publications

(9 citation statements)

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“…The results of this work demonstrate that the hydrolytic activity of the ATP synthase in R. cupsulutus can be strongly activated by sulfite. This observation extends previous studies in other organisms, such as other Rhodospirillaceae (Webster et al, 1977;Fregni and Casadio, 1993), archebacteria (Schobert, 1991(Schobert, , 1993 cyanobacteria (Bakels et al, 1994), higher plant choloroplaats Du and Boyer, 1990) and mitochondria (Moyle and Mitchell, 1975 ;Vasilyeva et a]., 1982;Cernyak et al, 1988). The activation by sulfite is therefore a general feature of all ATP synthases tested.…”

Section: Discussionsupporting

confidence: 87%

Sulfite Stimulates the ATP Hydrolysis Activity of but not Proton Translocation by the ATP Synthase of Rhodobacter Capsulatus and Interferes with its Activation by Δ_H+

Cappellini

Turina

Fregni

et al. 1997

European Journal of Biochemistry

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Sulfite stimulates the rate of ATP hydrolysis by the ATP synthase in chromatophores of Rhodobucter capsulatus. The stimulated activity is inhibited by oligomycin. The activation takes place also in uncoupled chromatophores. The activation consists in an increase of about 12-15-fold of the V,,,,, for the ATP hydrolysis reaction, while the K,,, for MgATP is unaffected at 0.16i0.03 mM. The dependence of V,,,,, on the sulfite concentration follows a hyperbolic pattern with half maximum effect at 12 mM.Sulfite affects the ability of the enzyme in translocating protons. Concomitant measurements of the rate of ATP hydrolysis and of ATP-induced protonic tlows demonstrate that at sulfite concentrations of greater than 10 mM the hydrolytic reaction becomes progressively uncoupled from the process of proton translocation. This is accompanied by an inhibition of ATP synthesis, either driven by light or by artificially induced ionic gradients. ATP synthesis is totally inhibited at concentrations of at least 80 mM.Sulfite interferes with the mechanism of activation by d P H , . Low concentrations of this anion ( S 2 mM) prevent the activation by A$,,+. At higher concentrations a marked stimulation of the activity prevails, regardless of the occurrence of a AFHt across the membrane. Phosphate at millimolar concentrations can reverse the inhibition by sulfite.These experimental results can be simulated by a model assuming multiple and competitive equilibria for phosphate or sulfite binding with two binding sites for the two ligands (for sulfite K,, = 0.26 and K2? = 37 mM, and for phosphate K , , = 0.06 and K2p = 4.22 mM), and in which the state bound only to one sulfite molecule is totally inactive in hydrolysis. The competition between phosphate and sulfite is igands and of the enzyme.ATP-driven proton translocation; protonic slipping; consistent with the molecular structures of the two

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Section: Discussionsupporting

confidence: 87%

Sulfite Stimulates the ATP Hydrolysis Activity of but not Proton Translocation by the ATP Synthase of Rhodobacter Capsulatus and Interferes with its Activation by Δ_H+

Cappellini

Turina

Fregni

et al. 1997

European Journal of Biochemistry

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“…Besides, the ATPase activity was not reduced by any of the ATPase inhibitors tested, N,NЈ-dicyclohexylcarbodiimide, thapsigargin, sodium orthovanadate, or oligomycin. No stimulating effect was observed in the presence of sodium sulfite (36).…”

Section: Fig 4 Analysis Of Subcellular Fractions From D1210(psu4053)mentioning

confidence: 83%

TrwD, a Protein Encoded by the IncW Plasmid R388, Displays an ATP Hydrolase Activity Essential for Bacterial Conjugation

Rivas¹,

Bolland²,

Cabezón³

et al. 1997

Journal of Biological Chemistry

113

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A 1.7-kilobase pair segment from the conjugative transfer region of plasmid R388 DNA was cloned and sequenced. It contained trwD, a gene essential for plasmid R388 conjugation, for expression of the conjugative W-pilus and for sensitivity to phage PRD1. The deduced amino acid sequence of TrwD showed homology to the PulE/VirB11 superfamily of potential ATPases involved in various types of transport processes. A fusion of trwD with the glutathione S-transferase (GST) was constructed, and the resulting fusion protein was purified from overproducing bacteria. Factor X a hydrolysis of GST-TrwD and further purification rendered TrwD protein with more than 95% purity. Antibodies raised against TrwD localized it both in the soluble fraction and in the outer membrane of Escherichia coli. TrwD is probably a peripheral outer membrane protein because it could be solubilized by increasing salt concentration to 0.5 M NaCl in the lysis buffer. Both purified GST-TrwD and TrwD could hydrolize ATP. ATPase activity increased 2-fold in the presence of detergent-phospholipid mixed micelles. To study the importance of the nucleotide-binding site, Walker box A (GXXGXGK(T/S)), present in TrwD, the conserved lysine residue was replaced by glutamine. The mutant protein, expressed and purified under the same conditions as the wild type, did not exhibit ATPase activity. TrwD(K203Q) was not able to complement the mutation in trwD of the R388 mutant plasmid, suggesting the essentiality of the ATPase activity of the protein in the conjugative process. Furthermore, the dominant character of this mutation suggested that GST-TrwD(K432Q) was still able to interact either with itself or with other component(s) of the conjugative machinery.

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“…It can also lead to SO 2 toxicity through sulfoxy-free radicals generated by the oxidation of SO 3 2- by O 2 − [23]. Furthermore, in membrane preparations of cyanobacteria, sulfite stimulates ATP hydrolysis and inhibits ATP synthesis [25]. Exogenous cysteine is believed to have direct effects on transporters and enzymes that are sensitive to thiol/disulfide redox variations [26].…”

Section: Discussionmentioning

confidence: 99%

Aerobic transformation of cadmium through metal sulfide biosynthesis in photosynthetic microorganisms

et al. 2013

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BackgroundCadmium is a non-essential metal that is toxic because of its interference with essential metals such as iron, calcium and zinc causing numerous detrimental metabolic and cellular effects. The amount of this metal in the environment has increased dramatically since the advent of the industrial age as a result of mining activities, the use of fertilizers and sewage sludge in farming, and discharges from manufacturing activities. The metal bioremediation utility of phototrophic microbes has been demonstrated through their ability to detoxify Hg(II) into HgS under aerobic conditions. Metal sulfides are generally very insoluble and therefore, biologically unavailable.ResultsWhen Cd(II) was exposed to cells it was bioconverted into CdS by the green alga Chlamydomonas reinhardtii, the red alga Cyanidioschyzon merolae, and the cyanobacterium, Synechoccocus leopoliensis. Supplementation of the two eukaryotic algae with extra sulfate, but not sulfite or cysteine, increased their cadmium tolerances as well as their abilities to produce CdS, indicating an involvement of sulfate assimilation in the detoxification process. However, the combined activities of extracted serine acetyl-transferase (SAT) and O-acetylserine(thiol)lyase (OASTL) used to monitor sulfate assimilation, was not significantly elevated during cell treatments that favored sulfide biosynthesis. It is possible that the prolonged incubation of the experiments occurring over two days could have compensated for the low rates of sulfate assimilation. This was also the case for S. leopoliensis where sulfite and cysteine as well as sulfate supplementation enhanced CdS synthesis. In general, conditions that increased cadmium sulfide production also resulted in elevated cysteine desulfhydrase activities, strongly suggesting that cysteine is the direct source of sulfur for CdS synthesis.ConclusionsCadmium(II) tolerance and CdS formation were significantly enhanced by sulfate supplementation, thus indicating that algae and cyanobacteria can produce CdS in a manner similar to that of HgS. Significant increases in sulfate assimilation as measured by SAT-OASTL activity were not detected. However, the enhanced activity of cysteine desulfhydrase indicates that it is instrumental in the provision of H2S for aerobic CdS biosynthesis.

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The Effect of Sulfite on the ATP Hydrolysis and Synthesis Activity of Membrane-Bound H+-ATP Synthase from Various Species

Cited by 19 publications

References 0 publications

Sulfite Stimulates the ATP Hydrolysis Activity of but not Proton Translocation by the ATP Synthase of Rhodobacter Capsulatus and Interferes with its Activation by Δ_H+

Sulfite Stimulates the ATP Hydrolysis Activity of but not Proton Translocation by the ATP Synthase of Rhodobacter Capsulatus and Interferes with its Activation by Δ_H+

TrwD, a Protein Encoded by the IncW Plasmid R388, Displays an ATP Hydrolase Activity Essential for Bacterial Conjugation

Aerobic transformation of cadmium through metal sulfide biosynthesis in photosynthetic microorganisms

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The Effect of Sulfite on the ATP Hydrolysis and Synthesis Activity of Membrane-Bound H+-ATP Synthase from Various Species

Cited by 19 publications

References 0 publications

Sulfite Stimulates the ATP Hydrolysis Activity of but not Proton Translocation by the ATP Synthase of Rhodobacter Capsulatus and Interferes with its Activation by ΔH+

Sulfite Stimulates the ATP Hydrolysis Activity of but not Proton Translocation by the ATP Synthase of Rhodobacter Capsulatus and Interferes with its Activation by ΔH+

TrwD, a Protein Encoded by the IncW Plasmid R388, Displays an ATP Hydrolase Activity Essential for Bacterial Conjugation

Aerobic transformation of cadmium through metal sulfide biosynthesis in photosynthetic microorganisms

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Sulfite Stimulates the ATP Hydrolysis Activity of but not Proton Translocation by the ATP Synthase of Rhodobacter Capsulatus and Interferes with its Activation by Δ_H+

Sulfite Stimulates the ATP Hydrolysis Activity of but not Proton Translocation by the ATP Synthase of Rhodobacter Capsulatus and Interferes with its Activation by Δ_H+