Enzymology and molecular biology of prokaryotic sulfite oxidation

Kappler, Ulrike; Dahl, Christiane

doi:10.1111/j.1574-6968.2001.tb10813.x

Cited by 160 publications

(116 citation statements)

References 61 publications

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“…3 and Table S3). In addition to the sulfur reducing Sox multienzyme complex, several enzymes known to oxidize sulfite to sulfate via the intermediate adenosine-5′-phosphosulfate in a Soxindependent pathway (22) were also encoded in the genome. The simultaneous presence of both sulfite-oxidizing pathways has also been observed in several other sulfur oxidizing bacteria, and is hypothesized to provide the organisms with a higher flexibility in their dissimilatory sulfur metabolism (22).…”

Section: Resultsmentioning

confidence: 99%

Genome and physiology of a model Epsilonproteobacterium responsible for sulfide detoxification in marine oxygen depletion zones

Grote

Schott

Brückner

et al. 2011

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

136

237

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Eutrophication and global climate change lead to expansion of hypoxia in the ocean, often accompanied by the production of hydrogen sulfide, which is toxic to higher organisms. Chemoautotrophic bacteria are thought to buffer against increased sulfide concentrations by oxidizing hydrogen sulfide before its diffusion to oxygenated surface waters. Model organisms from such environments have not been readily available, which has contributed to a poor understanding of these microbes. We present here a detailed study of "Sulfurimonas gotlandica" str. GD1, an Epsilonproteobacterium isolated from the Baltic Sea oxic-anoxic interface, where it plays a key role in nitrogen and sulfur cycling. Whole-genome analysis and laboratory experiments revealed a high metabolic flexibility, suggesting a considerable capacity for adaptation to variable redox conditions. S. gotlandica str. GD1 was shown to grow chemolithoautotrophically by coupling denitrification with oxidation of reduced sulfur compounds and dark CO 2 fixation. Metabolic versatility was further suggested by the use of a range of different electron donors and acceptors and organic carbon sources. The number of genes involved in signal transduction and metabolic pathways exceeds those of other Epsilonproteobacteria. Oxygen tolerance and environmental-sensing systems combined with chemotactic responses enable this organism to thrive successfully in marine oxygen-depletion zones. We propose that S. gotlandica str. GD1 will serve as a model organism in investigations that will lead to a better understanding how members of the Epsilonproteobacteria are able to cope with water column anoxia and the role these microorganisms play in the detoxification of sulfidic waters. marine bacteria | sulfide oxidation | isolation | genomics

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Section: Resultsmentioning

confidence: 99%

Genome and physiology of a model Epsilonproteobacterium responsible for sulfide detoxification in marine oxygen depletion zones

Grote

Schott

Brückner

et al. 2011

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

136

237

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“…There would appear to be no reports of sulfite oxidase [EC 1.8.3.1] in bacteria . There are, however, several different sulfite dehydrogenases [EC 1.8.2.1], but only one has been characterized, the cytochrome-c-coupled sulfite oxido-reductase (SorAB) from Starkeya novella (Kappler et al 2000;Kappler and Dahl 2001). The enzyme is periplasmic; SorA is a molybenum cofactor-containing dehydrogenase and SorB is a cytochrome c. Homologues of the sorAB genes are only now being found to be widespread in genome sequences.…”

Section: Fates Of the Sulfite Ionmentioning

confidence: 99%

Dissimilation of the C2 sulfonates

Cook

Denger

2002

Arch Microbiol

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Cysteate and sulfolactate are widespread natural products in the environment, while propanesulfonate, 3-aminopropanesulfonate and propane-1,3-disulfonate are xenobiotics. While some understanding of the bacterial assimilation of cysteate sulfur has been achieved, details of the dissimilation of cysteate and sulfolactate by microbes together with information on the degradation of the xenobiotics have only recently become available. This minireview centres on bacterial catabolism of the carbon moiety in these C 3 -sulfonates and on the fate of the sulfonate group. Three mechanisms of desulfonation have been established. Firstly, cysteate is converted via sulfopyruvate to sulfolactate, which is desulfonated to pyruvate and sulfite; the latter is oxidized to sulfate by a sulfite dehydrogenase and excreted as sulfate in Paracoccus pantotrophus NKN-CYSA. Secondly, sulfolactate can be converted to cysteate, which is cleaved in a pyridoxal 5¢-phosphatecoupled reaction to pyruvate, sulfite and ammonium ions; in Silicibacter pomeroyi DSS-3, the sulfite is excreted largely as sulfite. Both desulfonation reactions seem to be widespread. The third desulfonation mechanism is oxygenolysis of, e.g. propanesulfonate(s), about which less is known.

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“…APS reductase is a highly regulated enzyme, and it is considered to have a major control on the flux through assimilatory sulfate reduction in plants (3,15). However, the plant APS reductase is completely unrelated to the dissimilatory APS reductase found in both sulfate-reducing and sulfide-oxidizing bacteria and archaea (16,17). This dissimilatory APS reductase (EC 1.8.99.2) catalyzes both the reduction of APS to sulfite and the oxidation of sulfite and AMP to APS.…”

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confidence: 99%

The Presence of an Iron-Sulfur Cluster in Adenosine 5′-Phosphosulfate Reductase Separates Organisms Utilizing Adenosine 5′-Phosphosulfate and Phosphoadenosine 5′-Phosphosulfate for Sulfate Assimilation

Kopriva¹,

Büchert

Fritz

et al. 2002

Journal of Biological Chemistry

103

122

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It was generally accepted that plants, algae, and phototrophic bacteria use adenosine 5-phosphosulfate (APS) for assimilatory sulfate reduction, whereas bacteria and fungi use phosphoadenosine 5-phosphosulfate (PAPS). The corresponding enzymes, APS and PAPS reductase, share 25-30% identical amino acids. Phylogenetic analysis of APS and PAPS reductase amino acid sequences from different organisms, which were retrieved from the GenBank TM , revealed two clusters. The first cluster comprised known PAPS reductases from enteric bacteria, cyanobacteria, and yeast. On the other hand, plant APS reductase sequences were clustered together with many bacterial ones, including those from Pseudomonas and Rhizobium. The gene for APS reductase cloned from the APS-reducing cyanobacterium Plectonema also clustered together with the plant sequences, confirming that the two classes of sequences represent PAPS and APS reductases, respectively. Compared with the PAPS reductase, all sequences of the APS reductase cluster contained two additional cysteine pairs homologous to the cysteine residues involved in binding an iron-sulfur cluster in plants. Mö ssbauer analysis revealed that the recombinant APS reductase from Pseudomonas aeruginosa contains a [4Fe-4S] cluster with the same characteristics as the plant enzyme. We conclude, therefore, that the presence of an iron-sulfur cluster determines the APS specificity of the sulfatereducing enzymes and thus separates the APS-and PAPSdependent assimilatory sulfate reduction pathways.For all living organisms, sulfur is an essential element with many different functions. It is found in reduced form in amino acids, peptides, and proteins and in iron-sulfur clusters, lipoic acid, and other cofactors and in oxidized form as sulfonate group-modifying proteins, polysaccharides, and lipids. Reduced sulfur compounds, such as hydrogen sulfide, serve as electron donors for chemotrophic or phototrophic growth in a large and diverse group of Archae and bacteria, including purple and green sulfur bacteria (1). On the other hand, oxidized sulfur compounds such as sulfate can function as a terminal electron acceptor in respiration to support the growth of sulfate-reducing bacteria (2).The majority of sulfur in living organisms is present in the reduced form of organic thiols. For their synthesis, inorganic sulfate is reduced and incorporated into bioorganic compounds in a pathway named assimilatory sulfate reduction. Before reduction, sulfate is activated with ATP to adenosine 5Ј-phosphosulfate (APS), 1 which can subsequently be converted into phosphoadenosine 5Ј-phosphosulfate (PAPS) using a second ATP. Either form of activated sulfate can be reduced to sulfite and reduced further to sulfide by sulfite reductase. Sulfide is incorporated into an activated amino acid acceptor, such as O-acetylserine, O-acetylhomoserine, or O-succinylhomoserine, to form cysteine or homocysteine (3-5).The assimilatory sulfate reduction pathway is present in plants, fungi, and yeast and in a wide range of eubacteria but is mi...

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Enzymology and molecular biology of prokaryotic sulfite oxidation

Cited by 160 publications

References 61 publications

Genome and physiology of a model Epsilonproteobacterium responsible for sulfide detoxification in marine oxygen depletion zones

Genome and physiology of a model Epsilonproteobacterium responsible for sulfide detoxification in marine oxygen depletion zones

Dissimilation of the C2 sulfonates

The Presence of an Iron-Sulfur Cluster in Adenosine 5′-Phosphosulfate Reductase Separates Organisms Utilizing Adenosine 5′-Phosphosulfate and Phosphoadenosine 5′-Phosphosulfate for Sulfate Assimilation

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