a ferrooxidans strain atcc 23270 genome  (ATCC)


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    ATCC a ferrooxidans strain atcc 23270 genome
    Model of Fe(II) oxidation in A. ferrooxidans <t>ATCC</t> <t>23270</t> . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Extending the models for iron and sulfur oxidation in the extreme Acidophile Acidithiobacillus ferrooxidans"

    Article Title: Extending the models for iron and sulfur oxidation in the extreme Acidophile Acidithiobacillus ferrooxidans

    Journal: BMC Genomics

    doi: 10.1186/1471-2164-10-394

    Model of Fe(II) oxidation in A. ferrooxidans ATCC 23270 . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.
    Figure Legend Snippet: Model of Fe(II) oxidation in A. ferrooxidans ATCC 23270 . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.

    Techniques Used:


    Figure Legend Snippet: Microarray expression data for sulfur induced genes

    Techniques Used: Microarray, Expressing, Sequencing


    Figure Legend Snippet: Q-PCR expression data for relevant validated genes

    Techniques Used: Expressing, Transduction

    Model of sulfur oxidation in A. ferrooxidans ATCC 23270 . Reduced inorganic sulfur compound (RISC) oxidation pathways are predicted to involve various enzymes, enzyme complexes and a number of electron carriers located in different cellular compartments: in the outer membrane facing the periplasm (tetrathionate reductase, TetH), in the periplasm (high potential iron-sulfur protein, HiPIP), attached to the cytoplasmic membrane on the periplasmic side (cytochrome c , CycA2), in the cytoplasmic membrane (sulfide quinone reductase (SQR), thiosulfate quinone reductase (TQR), bc 1 complex, NADH complex I, bd and bo 3 terminal oxidases) and in the cytoplasm (heterodisulfide reductase (HDR), and ATP sulfurylase (SAT)). Insoluble sulfur is first converted to sulfane sulfate (GSSH) which is then transferred to the heterodisulfide reductase (HDR) through a cascade of sulfur transferases (DsrE, TusA and Rhd). Electrons coming from sulfide (H 2 S), thiosulfate (S 2 O 3 2- ) or sulfane sulfate (GSSH) are transferred via the quinol pool (QH 2 ) either (1) directly to terminal oxidases bd or bo 3 , or indirectly throught a bc 1 complex and a cytochrome c (CycA2) or a high potential iron-sulfur protein (HiPIP) probably to the aa 3 oxidase where O 2 reduction takes place or (2) to NADH complex I to generate reducing power.
    Figure Legend Snippet: Model of sulfur oxidation in A. ferrooxidans ATCC 23270 . Reduced inorganic sulfur compound (RISC) oxidation pathways are predicted to involve various enzymes, enzyme complexes and a number of electron carriers located in different cellular compartments: in the outer membrane facing the periplasm (tetrathionate reductase, TetH), in the periplasm (high potential iron-sulfur protein, HiPIP), attached to the cytoplasmic membrane on the periplasmic side (cytochrome c , CycA2), in the cytoplasmic membrane (sulfide quinone reductase (SQR), thiosulfate quinone reductase (TQR), bc 1 complex, NADH complex I, bd and bo 3 terminal oxidases) and in the cytoplasm (heterodisulfide reductase (HDR), and ATP sulfurylase (SAT)). Insoluble sulfur is first converted to sulfane sulfate (GSSH) which is then transferred to the heterodisulfide reductase (HDR) through a cascade of sulfur transferases (DsrE, TusA and Rhd). Electrons coming from sulfide (H 2 S), thiosulfate (S 2 O 3 2- ) or sulfane sulfate (GSSH) are transferred via the quinol pool (QH 2 ) either (1) directly to terminal oxidases bd or bo 3 , or indirectly throught a bc 1 complex and a cytochrome c (CycA2) or a high potential iron-sulfur protein (HiPIP) probably to the aa 3 oxidase where O 2 reduction takes place or (2) to NADH complex I to generate reducing power.

    Techniques Used:

    Comparison of the hdr cluster between A. ferrooxidans ATCC 23270 and other sulfur oxidizers . Heterodisulfide reductase complex (HdrC 1 B 1 AOrf2HdrC 2 B 2 ), accessory proteins (Rhd, TusA, DsrE) and ATP sulfurylase (Sat) in AF: A. ferrooxidans ATCC 23270 (NC_011206), AA: Aquifex aeolicus (NC_000918) and known acidophilic sulfur oxidizing microorganisms HB: Hydrogenobaculum sp. Y04AAS1 (NC_011126), HV: Hydrogenivirga sp. 128-5-R1-1 (NZ_ABHJ00000000), MS: Metallosphaera sedula (NC_009440), SA: Sulfolobus acidocaldarius (NC_007181), ST: S. tokodaii (NC_003106) and SS: S. solfataricus (NC_002754). Percentage of amino-acid similarity is indicated. Blue triangles represent inversion in the gene order.
    Figure Legend Snippet: Comparison of the hdr cluster between A. ferrooxidans ATCC 23270 and other sulfur oxidizers . Heterodisulfide reductase complex (HdrC 1 B 1 AOrf2HdrC 2 B 2 ), accessory proteins (Rhd, TusA, DsrE) and ATP sulfurylase (Sat) in AF: A. ferrooxidans ATCC 23270 (NC_011206), AA: Aquifex aeolicus (NC_000918) and known acidophilic sulfur oxidizing microorganisms HB: Hydrogenobaculum sp. Y04AAS1 (NC_011126), HV: Hydrogenivirga sp. 128-5-R1-1 (NZ_ABHJ00000000), MS: Metallosphaera sedula (NC_009440), SA: Sulfolobus acidocaldarius (NC_007181), ST: S. tokodaii (NC_003106) and SS: S. solfataricus (NC_002754). Percentage of amino-acid similarity is indicated. Blue triangles represent inversion in the gene order.

    Techniques Used:

    a ferrooxidans strain atcc 23270 genome  (ATCC)


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    ATCC a ferrooxidans strain atcc 23270 genome
    Model of Fe(II) oxidation in A. ferrooxidans <t>ATCC</t> <t>23270</t> . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Extending the models for iron and sulfur oxidation in the extreme Acidophile Acidithiobacillus ferrooxidans"

    Article Title: Extending the models for iron and sulfur oxidation in the extreme Acidophile Acidithiobacillus ferrooxidans

    Journal: BMC Genomics

    doi: 10.1186/1471-2164-10-394

    Model of Fe(II) oxidation in A. ferrooxidans ATCC 23270 . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.
    Figure Legend Snippet: Model of Fe(II) oxidation in A. ferrooxidans ATCC 23270 . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.

    Techniques Used:


    Figure Legend Snippet: Microarray expression data for sulfur induced genes

    Techniques Used: Microarray, Expressing, Sequencing


    Figure Legend Snippet: Q-PCR expression data for relevant validated genes

    Techniques Used: Expressing, Transduction

    Model of sulfur oxidation in A. ferrooxidans ATCC 23270 . Reduced inorganic sulfur compound (RISC) oxidation pathways are predicted to involve various enzymes, enzyme complexes and a number of electron carriers located in different cellular compartments: in the outer membrane facing the periplasm (tetrathionate reductase, TetH), in the periplasm (high potential iron-sulfur protein, HiPIP), attached to the cytoplasmic membrane on the periplasmic side (cytochrome c , CycA2), in the cytoplasmic membrane (sulfide quinone reductase (SQR), thiosulfate quinone reductase (TQR), bc 1 complex, NADH complex I, bd and bo 3 terminal oxidases) and in the cytoplasm (heterodisulfide reductase (HDR), and ATP sulfurylase (SAT)). Insoluble sulfur is first converted to sulfane sulfate (GSSH) which is then transferred to the heterodisulfide reductase (HDR) through a cascade of sulfur transferases (DsrE, TusA and Rhd). Electrons coming from sulfide (H 2 S), thiosulfate (S 2 O 3 2- ) or sulfane sulfate (GSSH) are transferred via the quinol pool (QH 2 ) either (1) directly to terminal oxidases bd or bo 3 , or indirectly throught a bc 1 complex and a cytochrome c (CycA2) or a high potential iron-sulfur protein (HiPIP) probably to the aa 3 oxidase where O 2 reduction takes place or (2) to NADH complex I to generate reducing power.
    Figure Legend Snippet: Model of sulfur oxidation in A. ferrooxidans ATCC 23270 . Reduced inorganic sulfur compound (RISC) oxidation pathways are predicted to involve various enzymes, enzyme complexes and a number of electron carriers located in different cellular compartments: in the outer membrane facing the periplasm (tetrathionate reductase, TetH), in the periplasm (high potential iron-sulfur protein, HiPIP), attached to the cytoplasmic membrane on the periplasmic side (cytochrome c , CycA2), in the cytoplasmic membrane (sulfide quinone reductase (SQR), thiosulfate quinone reductase (TQR), bc 1 complex, NADH complex I, bd and bo 3 terminal oxidases) and in the cytoplasm (heterodisulfide reductase (HDR), and ATP sulfurylase (SAT)). Insoluble sulfur is first converted to sulfane sulfate (GSSH) which is then transferred to the heterodisulfide reductase (HDR) through a cascade of sulfur transferases (DsrE, TusA and Rhd). Electrons coming from sulfide (H 2 S), thiosulfate (S 2 O 3 2- ) or sulfane sulfate (GSSH) are transferred via the quinol pool (QH 2 ) either (1) directly to terminal oxidases bd or bo 3 , or indirectly throught a bc 1 complex and a cytochrome c (CycA2) or a high potential iron-sulfur protein (HiPIP) probably to the aa 3 oxidase where O 2 reduction takes place or (2) to NADH complex I to generate reducing power.

    Techniques Used:

    Comparison of the hdr cluster between A. ferrooxidans ATCC 23270 and other sulfur oxidizers . Heterodisulfide reductase complex (HdrC 1 B 1 AOrf2HdrC 2 B 2 ), accessory proteins (Rhd, TusA, DsrE) and ATP sulfurylase (Sat) in AF: A. ferrooxidans ATCC 23270 (NC_011206), AA: Aquifex aeolicus (NC_000918) and known acidophilic sulfur oxidizing microorganisms HB: Hydrogenobaculum sp. Y04AAS1 (NC_011126), HV: Hydrogenivirga sp. 128-5-R1-1 (NZ_ABHJ00000000), MS: Metallosphaera sedula (NC_009440), SA: Sulfolobus acidocaldarius (NC_007181), ST: S. tokodaii (NC_003106) and SS: S. solfataricus (NC_002754). Percentage of amino-acid similarity is indicated. Blue triangles represent inversion in the gene order.
    Figure Legend Snippet: Comparison of the hdr cluster between A. ferrooxidans ATCC 23270 and other sulfur oxidizers . Heterodisulfide reductase complex (HdrC 1 B 1 AOrf2HdrC 2 B 2 ), accessory proteins (Rhd, TusA, DsrE) and ATP sulfurylase (Sat) in AF: A. ferrooxidans ATCC 23270 (NC_011206), AA: Aquifex aeolicus (NC_000918) and known acidophilic sulfur oxidizing microorganisms HB: Hydrogenobaculum sp. Y04AAS1 (NC_011126), HV: Hydrogenivirga sp. 128-5-R1-1 (NZ_ABHJ00000000), MS: Metallosphaera sedula (NC_009440), SA: Sulfolobus acidocaldarius (NC_007181), ST: S. tokodaii (NC_003106) and SS: S. solfataricus (NC_002754). Percentage of amino-acid similarity is indicated. Blue triangles represent inversion in the gene order.

    Techniques Used:

    a ferrooxidans strain atcc 23270 genome  (ATCC)


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    ATCC a ferrooxidans strain atcc 23270 genome
    General features of the <t> A. ferrooxidans ATCC 23270 genome. </t>
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications"

    Article Title: Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications

    Journal: BMC Genomics

    doi: 10.1186/1471-2164-9-597

    General features of the  A. ferrooxidans ATCC 23270 genome.
    Figure Legend Snippet: General features of the A. ferrooxidans ATCC 23270 genome.

    Techniques Used: Functional Assay, Binding Assay

    Circular representation of the A. ferrooxidans ATCC 23270 genome sequence . The two outer circles represent predicted protein encoding-genes on the forward and reverse strands, respectively. Functional categories are indicated by color, as follows: energy metabolism (green), DNA metabolism (red), protein synthesis (magenta), transcription (yellow), amino acid metabolism (orange), central intermediary metabolism (dark blue), cellular processes (light blue), nucleotide metabolism (turquoise), hypothetical and conserved hypothetical proteins (grey), mobile and extra-chromosomal elements (black), and general functions (brown). The third and fourth circles (forward and reverse strands) indicate major transposases and mobile elements (orange), plasmid-related genes (red), and phage elements (blue). The fifth and sixth circles (forward and reverse strands) indicate tRNA genes (gray). The seventh and eighth circles (forward and reverse strands) show genes predicted to be involved in sulfur (purple), iron (red), and hydrogen (orange) oxidation. The ninth and tenth circles show genomic GC bias and GC skew, respectively.
    Figure Legend Snippet: Circular representation of the A. ferrooxidans ATCC 23270 genome sequence . The two outer circles represent predicted protein encoding-genes on the forward and reverse strands, respectively. Functional categories are indicated by color, as follows: energy metabolism (green), DNA metabolism (red), protein synthesis (magenta), transcription (yellow), amino acid metabolism (orange), central intermediary metabolism (dark blue), cellular processes (light blue), nucleotide metabolism (turquoise), hypothetical and conserved hypothetical proteins (grey), mobile and extra-chromosomal elements (black), and general functions (brown). The third and fourth circles (forward and reverse strands) indicate major transposases and mobile elements (orange), plasmid-related genes (red), and phage elements (blue). The fifth and sixth circles (forward and reverse strands) indicate tRNA genes (gray). The seventh and eighth circles (forward and reverse strands) show genes predicted to be involved in sulfur (purple), iron (red), and hydrogen (orange) oxidation. The ninth and tenth circles show genomic GC bias and GC skew, respectively.

    Techniques Used: Sequencing, Functional Assay, Plasmid Preparation

    Whole-cell model for A. ferrooxidans ATCC 23270 . Genome-based model of the cellular metabolism of A. ferrooxidans including predicted transport systems; chemolithoautotrophic components; carbon, nitrogen and sulfur metabolism; and biogeochemical cycling.
    Figure Legend Snippet: Whole-cell model for A. ferrooxidans ATCC 23270 . Genome-based model of the cellular metabolism of A. ferrooxidans including predicted transport systems; chemolithoautotrophic components; carbon, nitrogen and sulfur metabolism; and biogeochemical cycling.

    Techniques Used:

    a ferrooxidans strain genomes  (ATCC)


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    ATCC a ferrooxidans strain genomes
    Scanning electron micrograph of Acidithiobacillus <t>ferrooxidans</t> YNTRS-40.
    A Ferrooxidans Strain Genomes, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Complete Genome Sequence of Acidithiobacillus ferrooxidans YNTRS-40, a Strain of the Ferrous Iron- and Sulfur-Oxidizing Acidophile"

    Article Title: Complete Genome Sequence of Acidithiobacillus ferrooxidans YNTRS-40, a Strain of the Ferrous Iron- and Sulfur-Oxidizing Acidophile

    Journal: Microorganisms

    doi: 10.3390/microorganisms8010002

    Scanning electron micrograph of Acidithiobacillus ferrooxidans YNTRS-40.
    Figure Legend Snippet: Scanning electron micrograph of Acidithiobacillus ferrooxidans YNTRS-40.

    Techniques Used:

    Circular chromosome genome map of Acidithiobacillus ferrooxidans YNTRS-40. (From the outside to the center, genes on direct strand, genes on complementary strand, tRNAs (orange), rRNAs (purple), CRISPR (blue), and genomic island (green), GC-skew, sequencing depth are displayed).
    Figure Legend Snippet: Circular chromosome genome map of Acidithiobacillus ferrooxidans YNTRS-40. (From the outside to the center, genes on direct strand, genes on complementary strand, tRNAs (orange), rRNAs (purple), CRISPR (blue), and genomic island (green), GC-skew, sequencing depth are displayed).

    Techniques Used: CRISPR, Sequencing

    Genome statistics of Acidithiobacillus  ferrooxidans  YNTRS-40.
    Figure Legend Snippet: Genome statistics of Acidithiobacillus ferrooxidans YNTRS-40.

    Techniques Used: CRISPR

    Phylogenetic tree based on the 16S rRNA gene sequence of Acidithiobacillus ferrooxidans YNTRS-40 and its relatives. Bootstrap values were calculated by MEGA7 using the neighbor-joining method from 1000 replications. Bar, 0.005 nucleotide substitutions per nucleotide position.
    Figure Legend Snippet: Phylogenetic tree based on the 16S rRNA gene sequence of Acidithiobacillus ferrooxidans YNTRS-40 and its relatives. Bootstrap values were calculated by MEGA7 using the neighbor-joining method from 1000 replications. Bar, 0.005 nucleotide substitutions per nucleotide position.

    Techniques Used: Sequencing

    a ferrooxidans strain genomes  (ATCC)


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    ATCC a ferrooxidans strain genomes
    A Ferrooxidans Strain Genomes, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    strain atcc 53993 genome  (ATCC)


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    ATCC strain atcc 53993 genome
    Strain Atcc 53993 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a ferrooxidans strain atcc 23270 genome  (ATCC)


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    ATCC a ferrooxidans strain atcc 23270 genome
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a ferrooxidans strain atcc 23270 genome  (ATCC)


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    ATCC a ferrooxidans strain atcc 23270 genome
    Purification of thiosulfate dehydrogenase at the optimal pH of 2.5 from the soluble fraction of tetrathionate-grown <t> A. ferrooxidans ATCC 23270 a </t>
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Tetrathionate-Forming Thiosulfate Dehydrogenase from the Acidophilic, Chemolithoautotrophic Bacterium Acidithiobacillus ferrooxidans"

    Article Title: Tetrathionate-Forming Thiosulfate Dehydrogenase from the Acidophilic, Chemolithoautotrophic Bacterium Acidithiobacillus ferrooxidans

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.02251-12

    Purification of thiosulfate dehydrogenase at the optimal pH of 2.5 from the soluble fraction of tetrathionate-grown  A. ferrooxidans ATCC 23270 a
    Figure Legend Snippet: Purification of thiosulfate dehydrogenase at the optimal pH of 2.5 from the soluble fraction of tetrathionate-grown A. ferrooxidans ATCC 23270 a

    Techniques Used: Purification, Activity Assay

    SDS-PAGE of partially purified thiosulfate dehydrogenase. (A) Lanes 1 to 5, samples from A. ferrooxidans ATCC 23270. (B) Lanes 7 to 9, samples from E. coli BL21(DE3) harboring pET-tsd. Lane 1, cell extract (20 μg); lane 2, soluble fraction (6.8 μg); lane 3, soluble fraction at pH 4 (11.35 μg); lane 4, CM-650M fraction (1.58 μg); lane 5, Butyl-650M fraction (1.04 μg); lane M, molecular markers; lane 6, cell extract from E. coli with pET21a (10 μg); lane 7, cell extract (9.9 μg); lane 8, soluble protein at pH 4.0 (9.9 μg); lane 9, Butyl-650M fraction (1.53 μg).
    Figure Legend Snippet: SDS-PAGE of partially purified thiosulfate dehydrogenase. (A) Lanes 1 to 5, samples from A. ferrooxidans ATCC 23270. (B) Lanes 7 to 9, samples from E. coli BL21(DE3) harboring pET-tsd. Lane 1, cell extract (20 μg); lane 2, soluble fraction (6.8 μg); lane 3, soluble fraction at pH 4 (11.35 μg); lane 4, CM-650M fraction (1.58 μg); lane 5, Butyl-650M fraction (1.04 μg); lane M, molecular markers; lane 6, cell extract from E. coli with pET21a (10 μg); lane 7, cell extract (9.9 μg); lane 8, soluble protein at pH 4.0 (9.9 μg); lane 9, Butyl-650M fraction (1.53 μg).

    Techniques Used: SDS Page, Purification

    Time course of absorbance changes at 420 nm after mixing thiosulfate or sulfite and ferricyanide in the presence or absence of enzyme. Symbols: ●, thiosulfate and enzyme; ○, thiosulfate and heat-denatured enzyme; □, thiosulfate and water; ▲, sulfite and enzyme; △, only enzyme without substrates. Experiments were carried out at pH 2.5 and 40°C in triplicates in a mixture containing 1 mM ferricyanide, 10 mM Na-thiosulfate or 10 mM Na-sulfite, 50 mM Na-sulfate, and 7 μg of protein ml−1 (Butyl-650M fraction) from A. ferrooxidans ATCC 23270.
    Figure Legend Snippet: Time course of absorbance changes at 420 nm after mixing thiosulfate or sulfite and ferricyanide in the presence or absence of enzyme. Symbols: ●, thiosulfate and enzyme; ○, thiosulfate and heat-denatured enzyme; □, thiosulfate and water; ▲, sulfite and enzyme; △, only enzyme without substrates. Experiments were carried out at pH 2.5 and 40°C in triplicates in a mixture containing 1 mM ferricyanide, 10 mM Na-thiosulfate or 10 mM Na-sulfite, 50 mM Na-sulfate, and 7 μg of protein ml−1 (Butyl-650M fraction) from A. ferrooxidans ATCC 23270.

    Techniques Used:

    Effect of sulfate (A), sulfite (B), pH (C), or temperature (D) on TSD activity in Butyl-650M fraction from A. ferrooxidans ATCC 23270 (●) or E. coli BL21(DE3) harboring pET-tsd (○). The effect of sulfate on TSD activity in CM-650M fraction is represented by a black square (■) in panel A. The specific activities (U mg−1) for the 100% value are indicated in the four panels as follows: 3.47 (●), 4.57 (○), and 2.34 (■) (A); 5.47 (●) and 4.57 (○) (B); 3.47 (●) and 4.57 (○) (C); and 13.79 (●) and 6.53 (○) (D).
    Figure Legend Snippet: Effect of sulfate (A), sulfite (B), pH (C), or temperature (D) on TSD activity in Butyl-650M fraction from A. ferrooxidans ATCC 23270 (●) or E. coli BL21(DE3) harboring pET-tsd (○). The effect of sulfate on TSD activity in CM-650M fraction is represented by a black square (■) in panel A. The specific activities (U mg−1) for the 100% value are indicated in the four panels as follows: 3.47 (●), 4.57 (○), and 2.34 (■) (A); 5.47 (●) and 4.57 (○) (B); 3.47 (●) and 4.57 (○) (C); and 13.79 (●) and 6.53 (○) (D).

    Techniques Used: Activity Assay

    Effect of thiosulfate concentration on TSD activity in the Butyl-650M fraction of A. ferrooxidans ATCC 23270 (●) or E. coli BL21(DE3) harboring pET-tsd (○). Experiments were carried out at pH 2.5 and 40°C in a mixture containing 1 mM ferricyanide and 50 mM Na-sulfate.
    Figure Legend Snippet: Effect of thiosulfate concentration on TSD activity in the Butyl-650M fraction of A. ferrooxidans ATCC 23270 (●) or E. coli BL21(DE3) harboring pET-tsd (○). Experiments were carried out at pH 2.5 and 40°C in a mixture containing 1 mM ferricyanide and 50 mM Na-sulfate.

    Techniques Used: Concentration Assay, Activity Assay

    a ferrooxidans strain atcc 23270 genome  (ATCC)


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    ATCC a ferrooxidans strain atcc 23270 genome
    Purification of thiosulfate dehydrogenase at the optimal pH of 2.5 from the soluble fraction of tetrathionate-grown <t> A. ferrooxidans ATCC 23270 a </t>
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Tetrathionate-Forming Thiosulfate Dehydrogenase from the Acidophilic, Chemolithoautotrophic Bacterium Acidithiobacillus ferrooxidans"

    Article Title: Tetrathionate-Forming Thiosulfate Dehydrogenase from the Acidophilic, Chemolithoautotrophic Bacterium Acidithiobacillus ferrooxidans

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.02251-12

    Purification of thiosulfate dehydrogenase at the optimal pH of 2.5 from the soluble fraction of tetrathionate-grown  A. ferrooxidans ATCC 23270 a
    Figure Legend Snippet: Purification of thiosulfate dehydrogenase at the optimal pH of 2.5 from the soluble fraction of tetrathionate-grown A. ferrooxidans ATCC 23270 a

    Techniques Used: Purification, Activity Assay

    SDS-PAGE of partially purified thiosulfate dehydrogenase. (A) Lanes 1 to 5, samples from A. ferrooxidans ATCC 23270. (B) Lanes 7 to 9, samples from E. coli BL21(DE3) harboring pET-tsd. Lane 1, cell extract (20 μg); lane 2, soluble fraction (6.8 μg); lane 3, soluble fraction at pH 4 (11.35 μg); lane 4, CM-650M fraction (1.58 μg); lane 5, Butyl-650M fraction (1.04 μg); lane M, molecular markers; lane 6, cell extract from E. coli with pET21a (10 μg); lane 7, cell extract (9.9 μg); lane 8, soluble protein at pH 4.0 (9.9 μg); lane 9, Butyl-650M fraction (1.53 μg).
    Figure Legend Snippet: SDS-PAGE of partially purified thiosulfate dehydrogenase. (A) Lanes 1 to 5, samples from A. ferrooxidans ATCC 23270. (B) Lanes 7 to 9, samples from E. coli BL21(DE3) harboring pET-tsd. Lane 1, cell extract (20 μg); lane 2, soluble fraction (6.8 μg); lane 3, soluble fraction at pH 4 (11.35 μg); lane 4, CM-650M fraction (1.58 μg); lane 5, Butyl-650M fraction (1.04 μg); lane M, molecular markers; lane 6, cell extract from E. coli with pET21a (10 μg); lane 7, cell extract (9.9 μg); lane 8, soluble protein at pH 4.0 (9.9 μg); lane 9, Butyl-650M fraction (1.53 μg).

    Techniques Used: SDS Page, Purification

    Time course of absorbance changes at 420 nm after mixing thiosulfate or sulfite and ferricyanide in the presence or absence of enzyme. Symbols: ●, thiosulfate and enzyme; ○, thiosulfate and heat-denatured enzyme; □, thiosulfate and water; ▲, sulfite and enzyme; △, only enzyme without substrates. Experiments were carried out at pH 2.5 and 40°C in triplicates in a mixture containing 1 mM ferricyanide, 10 mM Na-thiosulfate or 10 mM Na-sulfite, 50 mM Na-sulfate, and 7 μg of protein ml−1 (Butyl-650M fraction) from A. ferrooxidans ATCC 23270.
    Figure Legend Snippet: Time course of absorbance changes at 420 nm after mixing thiosulfate or sulfite and ferricyanide in the presence or absence of enzyme. Symbols: ●, thiosulfate and enzyme; ○, thiosulfate and heat-denatured enzyme; □, thiosulfate and water; ▲, sulfite and enzyme; △, only enzyme without substrates. Experiments were carried out at pH 2.5 and 40°C in triplicates in a mixture containing 1 mM ferricyanide, 10 mM Na-thiosulfate or 10 mM Na-sulfite, 50 mM Na-sulfate, and 7 μg of protein ml−1 (Butyl-650M fraction) from A. ferrooxidans ATCC 23270.

    Techniques Used:

    Effect of sulfate (A), sulfite (B), pH (C), or temperature (D) on TSD activity in Butyl-650M fraction from A. ferrooxidans ATCC 23270 (●) or E. coli BL21(DE3) harboring pET-tsd (○). The effect of sulfate on TSD activity in CM-650M fraction is represented by a black square (■) in panel A. The specific activities (U mg−1) for the 100% value are indicated in the four panels as follows: 3.47 (●), 4.57 (○), and 2.34 (■) (A); 5.47 (●) and 4.57 (○) (B); 3.47 (●) and 4.57 (○) (C); and 13.79 (●) and 6.53 (○) (D).
    Figure Legend Snippet: Effect of sulfate (A), sulfite (B), pH (C), or temperature (D) on TSD activity in Butyl-650M fraction from A. ferrooxidans ATCC 23270 (●) or E. coli BL21(DE3) harboring pET-tsd (○). The effect of sulfate on TSD activity in CM-650M fraction is represented by a black square (■) in panel A. The specific activities (U mg−1) for the 100% value are indicated in the four panels as follows: 3.47 (●), 4.57 (○), and 2.34 (■) (A); 5.47 (●) and 4.57 (○) (B); 3.47 (●) and 4.57 (○) (C); and 13.79 (●) and 6.53 (○) (D).

    Techniques Used: Activity Assay

    Effect of thiosulfate concentration on TSD activity in the Butyl-650M fraction of A. ferrooxidans ATCC 23270 (●) or E. coli BL21(DE3) harboring pET-tsd (○). Experiments were carried out at pH 2.5 and 40°C in a mixture containing 1 mM ferricyanide and 50 mM Na-sulfate.
    Figure Legend Snippet: Effect of thiosulfate concentration on TSD activity in the Butyl-650M fraction of A. ferrooxidans ATCC 23270 (●) or E. coli BL21(DE3) harboring pET-tsd (○). Experiments were carried out at pH 2.5 and 40°C in a mixture containing 1 mM ferricyanide and 50 mM Na-sulfate.

    Techniques Used: Concentration Assay, Activity Assay

    a ferrooxidans strain atcc 23270 genome  (ATCC)


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    ATCC a ferrooxidans strain atcc 23270 genome
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    a ferrooxidans strain atcc 23270 genome  (ATCC)


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    ATCC a ferrooxidans strain atcc 23270 genome
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC a ferrooxidans strain atcc 23270 genome
    Model of Fe(II) oxidation in A. ferrooxidans <t>ATCC</t> <t>23270</t> . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.
    A Ferrooxidans Strain Atcc 23270 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC a ferrooxidans strain genomes
    Scanning electron micrograph of Acidithiobacillus <t>ferrooxidans</t> YNTRS-40.
    A Ferrooxidans Strain Genomes, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC strain atcc 53993 genome
    Scanning electron micrograph of Acidithiobacillus <t>ferrooxidans</t> YNTRS-40.
    Strain Atcc 53993 Genome, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Model of Fe(II) oxidation in A. ferrooxidans ATCC 23270 . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.

    Journal: BMC Genomics

    Article Title: Extending the models for iron and sulfur oxidation in the extreme Acidophile Acidithiobacillus ferrooxidans

    doi: 10.1186/1471-2164-10-394

    Figure Lengend Snippet: Model of Fe(II) oxidation in A. ferrooxidans ATCC 23270 . The flow of electrons is shown from the oxidation of Fe +2 by Cyc2 to reduce oxygen via the aa 3 complex (downhill pathway) or to reduce NAD+ via bc 1 /quinone pool/NADH complex (uphill pathway). The downhill pathway can consume protons entering via the ATPase complex helping to drive ATP synthesis or via the bc 1 /quinone pool/NADH complex that drives the flow of electrons in the uphill pathway. The switch point between the downhill and uphill flow is suggested to be at the level of rusticyanin (Rus). Abbreviations used can be found in the text.

    Article Snippet: The sequence and annotation of the complete A. ferrooxidans strain ATCC 23270 genome was retrieved from GenBank/EMBL/DDBJ ( CP001219 ).

    Techniques:

    Journal: BMC Genomics

    Article Title: Extending the models for iron and sulfur oxidation in the extreme Acidophile Acidithiobacillus ferrooxidans

    doi: 10.1186/1471-2164-10-394

    Figure Lengend Snippet: Microarray expression data for sulfur induced genes

    Article Snippet: The sequence and annotation of the complete A. ferrooxidans strain ATCC 23270 genome was retrieved from GenBank/EMBL/DDBJ ( CP001219 ).

    Techniques: Microarray, Expressing, Sequencing

    Model of sulfur oxidation in A. ferrooxidans ATCC 23270 . Reduced inorganic sulfur compound (RISC) oxidation pathways are predicted to involve various enzymes, enzyme complexes and a number of electron carriers located in different cellular compartments: in the outer membrane facing the periplasm (tetrathionate reductase, TetH), in the periplasm (high potential iron-sulfur protein, HiPIP), attached to the cytoplasmic membrane on the periplasmic side (cytochrome c , CycA2), in the cytoplasmic membrane (sulfide quinone reductase (SQR), thiosulfate quinone reductase (TQR), bc 1 complex, NADH complex I, bd and bo 3 terminal oxidases) and in the cytoplasm (heterodisulfide reductase (HDR), and ATP sulfurylase (SAT)). Insoluble sulfur is first converted to sulfane sulfate (GSSH) which is then transferred to the heterodisulfide reductase (HDR) through a cascade of sulfur transferases (DsrE, TusA and Rhd). Electrons coming from sulfide (H 2 S), thiosulfate (S 2 O 3 2- ) or sulfane sulfate (GSSH) are transferred via the quinol pool (QH 2 ) either (1) directly to terminal oxidases bd or bo 3 , or indirectly throught a bc 1 complex and a cytochrome c (CycA2) or a high potential iron-sulfur protein (HiPIP) probably to the aa 3 oxidase where O 2 reduction takes place or (2) to NADH complex I to generate reducing power.

    Journal: BMC Genomics

    Article Title: Extending the models for iron and sulfur oxidation in the extreme Acidophile Acidithiobacillus ferrooxidans

    doi: 10.1186/1471-2164-10-394

    Figure Lengend Snippet: Model of sulfur oxidation in A. ferrooxidans ATCC 23270 . Reduced inorganic sulfur compound (RISC) oxidation pathways are predicted to involve various enzymes, enzyme complexes and a number of electron carriers located in different cellular compartments: in the outer membrane facing the periplasm (tetrathionate reductase, TetH), in the periplasm (high potential iron-sulfur protein, HiPIP), attached to the cytoplasmic membrane on the periplasmic side (cytochrome c , CycA2), in the cytoplasmic membrane (sulfide quinone reductase (SQR), thiosulfate quinone reductase (TQR), bc 1 complex, NADH complex I, bd and bo 3 terminal oxidases) and in the cytoplasm (heterodisulfide reductase (HDR), and ATP sulfurylase (SAT)). Insoluble sulfur is first converted to sulfane sulfate (GSSH) which is then transferred to the heterodisulfide reductase (HDR) through a cascade of sulfur transferases (DsrE, TusA and Rhd). Electrons coming from sulfide (H 2 S), thiosulfate (S 2 O 3 2- ) or sulfane sulfate (GSSH) are transferred via the quinol pool (QH 2 ) either (1) directly to terminal oxidases bd or bo 3 , or indirectly throught a bc 1 complex and a cytochrome c (CycA2) or a high potential iron-sulfur protein (HiPIP) probably to the aa 3 oxidase where O 2 reduction takes place or (2) to NADH complex I to generate reducing power.

    Article Snippet: The sequence and annotation of the complete A. ferrooxidans strain ATCC 23270 genome was retrieved from GenBank/EMBL/DDBJ ( CP001219 ).

    Techniques:

    Comparison of the hdr cluster between A. ferrooxidans ATCC 23270 and other sulfur oxidizers . Heterodisulfide reductase complex (HdrC 1 B 1 AOrf2HdrC 2 B 2 ), accessory proteins (Rhd, TusA, DsrE) and ATP sulfurylase (Sat) in AF: A. ferrooxidans ATCC 23270 (NC_011206), AA: Aquifex aeolicus (NC_000918) and known acidophilic sulfur oxidizing microorganisms HB: Hydrogenobaculum sp. Y04AAS1 (NC_011126), HV: Hydrogenivirga sp. 128-5-R1-1 (NZ_ABHJ00000000), MS: Metallosphaera sedula (NC_009440), SA: Sulfolobus acidocaldarius (NC_007181), ST: S. tokodaii (NC_003106) and SS: S. solfataricus (NC_002754). Percentage of amino-acid similarity is indicated. Blue triangles represent inversion in the gene order.

    Journal: BMC Genomics

    Article Title: Extending the models for iron and sulfur oxidation in the extreme Acidophile Acidithiobacillus ferrooxidans

    doi: 10.1186/1471-2164-10-394

    Figure Lengend Snippet: Comparison of the hdr cluster between A. ferrooxidans ATCC 23270 and other sulfur oxidizers . Heterodisulfide reductase complex (HdrC 1 B 1 AOrf2HdrC 2 B 2 ), accessory proteins (Rhd, TusA, DsrE) and ATP sulfurylase (Sat) in AF: A. ferrooxidans ATCC 23270 (NC_011206), AA: Aquifex aeolicus (NC_000918) and known acidophilic sulfur oxidizing microorganisms HB: Hydrogenobaculum sp. Y04AAS1 (NC_011126), HV: Hydrogenivirga sp. 128-5-R1-1 (NZ_ABHJ00000000), MS: Metallosphaera sedula (NC_009440), SA: Sulfolobus acidocaldarius (NC_007181), ST: S. tokodaii (NC_003106) and SS: S. solfataricus (NC_002754). Percentage of amino-acid similarity is indicated. Blue triangles represent inversion in the gene order.

    Article Snippet: The sequence and annotation of the complete A. ferrooxidans strain ATCC 23270 genome was retrieved from GenBank/EMBL/DDBJ ( CP001219 ).

    Techniques:

    Scanning electron micrograph of Acidithiobacillus ferrooxidans YNTRS-40.

    Journal: Microorganisms

    Article Title: Complete Genome Sequence of Acidithiobacillus ferrooxidans YNTRS-40, a Strain of the Ferrous Iron- and Sulfur-Oxidizing Acidophile

    doi: 10.3390/microorganisms8010002

    Figure Lengend Snippet: Scanning electron micrograph of Acidithiobacillus ferrooxidans YNTRS-40.

    Article Snippet: Until now, nine A. ferrooxidans strain genomes (ATCC 23270, ATCC 53993, Hel18, BY0502, CCM 4253, IO-2C, YQH-1, DLC-5, and RVS1) have been available in the public databases.

    Techniques:

    Circular chromosome genome map of Acidithiobacillus ferrooxidans YNTRS-40. (From the outside to the center, genes on direct strand, genes on complementary strand, tRNAs (orange), rRNAs (purple), CRISPR (blue), and genomic island (green), GC-skew, sequencing depth are displayed).

    Journal: Microorganisms

    Article Title: Complete Genome Sequence of Acidithiobacillus ferrooxidans YNTRS-40, a Strain of the Ferrous Iron- and Sulfur-Oxidizing Acidophile

    doi: 10.3390/microorganisms8010002

    Figure Lengend Snippet: Circular chromosome genome map of Acidithiobacillus ferrooxidans YNTRS-40. (From the outside to the center, genes on direct strand, genes on complementary strand, tRNAs (orange), rRNAs (purple), CRISPR (blue), and genomic island (green), GC-skew, sequencing depth are displayed).

    Article Snippet: Until now, nine A. ferrooxidans strain genomes (ATCC 23270, ATCC 53993, Hel18, BY0502, CCM 4253, IO-2C, YQH-1, DLC-5, and RVS1) have been available in the public databases.

    Techniques: CRISPR, Sequencing

    Genome statistics of Acidithiobacillus  ferrooxidans  YNTRS-40.

    Journal: Microorganisms

    Article Title: Complete Genome Sequence of Acidithiobacillus ferrooxidans YNTRS-40, a Strain of the Ferrous Iron- and Sulfur-Oxidizing Acidophile

    doi: 10.3390/microorganisms8010002

    Figure Lengend Snippet: Genome statistics of Acidithiobacillus ferrooxidans YNTRS-40.

    Article Snippet: Until now, nine A. ferrooxidans strain genomes (ATCC 23270, ATCC 53993, Hel18, BY0502, CCM 4253, IO-2C, YQH-1, DLC-5, and RVS1) have been available in the public databases.

    Techniques: CRISPR

    Phylogenetic tree based on the 16S rRNA gene sequence of Acidithiobacillus ferrooxidans YNTRS-40 and its relatives. Bootstrap values were calculated by MEGA7 using the neighbor-joining method from 1000 replications. Bar, 0.005 nucleotide substitutions per nucleotide position.

    Journal: Microorganisms

    Article Title: Complete Genome Sequence of Acidithiobacillus ferrooxidans YNTRS-40, a Strain of the Ferrous Iron- and Sulfur-Oxidizing Acidophile

    doi: 10.3390/microorganisms8010002

    Figure Lengend Snippet: Phylogenetic tree based on the 16S rRNA gene sequence of Acidithiobacillus ferrooxidans YNTRS-40 and its relatives. Bootstrap values were calculated by MEGA7 using the neighbor-joining method from 1000 replications. Bar, 0.005 nucleotide substitutions per nucleotide position.

    Article Snippet: Until now, nine A. ferrooxidans strain genomes (ATCC 23270, ATCC 53993, Hel18, BY0502, CCM 4253, IO-2C, YQH-1, DLC-5, and RVS1) have been available in the public databases.

    Techniques: Sequencing