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Enzyme Nomenclature
Information on EC 1.16.9.1 - iron:rusticyanin reductase
for references in articles please use BRENDA:EC1.16.9.1
Word Map on EC 1.16.9.1
- 1.16.9.1
- vulgaris
-
desulfovibrio
- hildenborough
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periplasmic
- hemes
- ferrooxidans
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thiobacillus
- nitrate
-
shewanella
-
high-spin
-
c4-type
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hydrogenase
-
miyazaki
-
low-spin
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holoproteins
- desulfuricans
- epr
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ferrous
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The expected taxonomic range for this enzyme is: Acidithiobacillus ferrooxidans
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EC NUMBER 
COMMENTARY 
1.16.9.1
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RECOMMENDED NAME
GeneOntology No.
iron:rusticyanin reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Fe(II) + rusticyanin = Fe(III) + reduced rusticyanin
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
Fe(II):rusticyanin oxidoreductase
Contains c-type heme. The enzyme in Acidithiobacillus ferrooxidans is a component of an electron transfer chain from Fe(II), comprising this enzyme, the copper protein rusticyanin, cytochrome c4, and cytochrome c oxidase (EC 1.9.3.1).
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
strain CCM 4253 shows 100% identity to type strain ATCC 23270
UniProt
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
strain CCM 4253 shows 100% identity to type strain ATCC 23270
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
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exclusive sulfur oxidizers such as Acidithiobacillus thiooxidans and Acidithiobacillus caldus cannot oxidize S0 under anaerobic conditions. The ability to facultatively oxidize S0 with Fe3+ as the electron acceptor in oxygen-limited environments has only been demonstrated in sulfur and iron oxidizers such as Acidithiobacillus ferrooxidans, Acidithiobacillus ferridurans, Acidithiobacillus ferrivorans and Acidithiobacillus ferriphilus strains, all previously generally classified as different strains of Acidithiobacillus ferrooxidans (Group I-IV)
evolution
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
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exclusive sulfur oxidizers such as Acidithiobacillus thiooxidans and Acidithiobacillus caldus cannot oxidize S0 under anaerobic conditions. The ability to facultatively oxidize S0 with Fe3+ as the electron acceptor in oxygen-limited environments has only been demonstrated in sulfur and iron oxidizers such as Acidithiobacillus ferrooxidans, Acidithiobacillus ferridurans, Acidithiobacillus ferrivorans and Acidithiobacillus ferriphilus strains, all previously generally classified as different strains of Acidithiobacillus ferrooxidans (Group I-IV)
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malfunction
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by overexpression of Cyc2 in Acidithiobacillus ferrooxidans Fe2+ oxidation activity and arsenic stressed cell growth is increased
malfunction
cells lacking the Fe3+-reducing capacity reveal downregulation of energy metabolism proteins, which are in some cases even absent. Among the repressed and missing proteins are Cyc2, rusticyanin, heterodisulfide reductase (Hdr), thiosulfate:quinone oxidoreductase (Tqo) and sulfide:quinone reductase (Sqr)
malfunction
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
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cells lacking the Fe3+-reducing capacity reveal downregulation of energy metabolism proteins, which are in some cases even absent. Among the repressed and missing proteins are Cyc2, rusticyanin, heterodisulfide reductase (Hdr), thiosulfate:quinone oxidoreductase (Tqo) and sulfide:quinone reductase (Sqr)
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metabolism
the enzyme is involved in the involved in the anaerobic pathway of S0 oxidation coupled with dissimilatory Fe3+ reduction. The pathway of anaerobic sulfur oxidation coupled with dissimilatory ferric iron reduction in Acidithiobacillus ferrooxidans strain CCM 4253. The main proposed mechanism involves: outer membrane protein Cyc2 (assumed to function as a terminal ferric iron reductase), periplasmic electron shuttle rusticyanin, c4-type cytochrome CycA1, the inner membrane cytochrome bc1 complex I, and the quinone pool providing connection to the sulfur metabolism machinery, consisting of heterodisulfide reductase, thiosulfate:quinone oxidoreductase and tetrathionate hydrolase. An alternative mechanism seems to involve a high potential iron-sulfur protein Hip, c4-type cytochrome CycA2 and inner membrane cytochrome bc1 complex II. Strain- or phenotype-dependent pathway variation, overview. The enzyme is involved in the anaerobic respiratory pathway, regulation of the pathway and model overview
metabolism
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the main anaerobic respiratory pathway includes the cytochrome bc1 complex I, a c4-type cytochrome, rusticyanin, and Cyc2 as the terminal reductase. Analysis of Fe3+-reducing activity of Acidithiobacillus ferrooxidans strain CCM 4253 phenotypes in resting cell suspension cultures, transcriptomic and proteomic analysis and modeling of wild-type and of S0-grown subcultures that have lost the ability to reduce Fe3+, overview
metabolism
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
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the enzyme is involved in the involved in the anaerobic pathway of S0 oxidation coupled with dissimilatory Fe3+ reduction. The pathway of anaerobic sulfur oxidation coupled with dissimilatory ferric iron reduction in Acidithiobacillus ferrooxidans strain CCM 4253. The main proposed mechanism involves: outer membrane protein Cyc2 (assumed to function as a terminal ferric iron reductase), periplasmic electron shuttle rusticyanin, c4-type cytochrome CycA1, the inner membrane cytochrome bc1 complex I, and the quinone pool providing connection to the sulfur metabolism machinery, consisting of heterodisulfide reductase, thiosulfate:quinone oxidoreductase and tetrathionate hydrolase. An alternative mechanism seems to involve a high potential iron-sulfur protein Hip, c4-type cytochrome CycA2 and inner membrane cytochrome bc1 complex II. Strain- or phenotype-dependent pathway variation, overview. The enzyme is involved in the anaerobic respiratory pathway, regulation of the pathway and model overview; the main anaerobic respiratory pathway includes the cytochrome bc1 complex I, a c4-type cytochrome, rusticyanin, and Cyc2 as the terminal reductase. Analysis of Fe3+-reducing activity of Acidithiobacillus ferrooxidans strain CCM 4253 phenotypes in resting cell suspension cultures, transcriptomic and proteomic analysis and modeling of wild-type and of S0-grown subcultures that have lost the ability to reduce Fe3+, overview
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physiological function
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the iron:rusticyanin oxidoreductase is the primary cellular oxidant of ferrous ions in the iron respiratory electron transport chain of Thiobacillus ferrooxidans
physiological function
ability of Acidithiobacillus ferrooxidans to anaerobically reduce Fe3+, molecular mechanism, overview. Rusticyanin is a stable and highly abundant protein in Fe2+-grown cells, in which it represents about 5% of soluble protein, that fulfills the role of an electron transporter in the respiratory chain, even after strong reduction of its content in a cell. The terminal Fe3+ reductase might be outer membrane cytochrome Cyc2, operating in reverse mode and reducing Fe3+ to Fe2+ under anaerobic conditions
physiological function
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
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ability of Acidithiobacillus ferrooxidans to anaerobically reduce Fe3+, molecular mechanism, overview. Rusticyanin is a stable and highly abundant protein in Fe2+-grown cells, in which it represents about 5% of soluble protein, that fulfills the role of an electron transporter in the respiratory chain, even after strong reduction of its content in a cell. The terminal Fe3+ reductase might be outer membrane cytochrome Cyc2, operating in reverse mode and reducing Fe3+ to Fe2+ under anaerobic conditions
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
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-
-
-
?
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
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-
-
?
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
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-
-
-
?
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
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-
-
?
additional information
?
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direct interaction between rusticyanin and Cyc2, but no interaction between Cyc2 and c4-type cytochrome Cyc1 or c4-type cytochrome CycA1
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-
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additional information
?
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Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
direct interaction between rusticyanin and Cyc2, but no interaction between Cyc2 and c4-type cytochrome Cyc1 or c4-type cytochrome CycA1
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
O33823
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-
-
?
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
O33823
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-
-
?
additional information
?
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O33823
direct interaction between rusticyanin and Cyc2, but no interaction between Cyc2 and c4-type cytochrome Cyc1 or c4-type cytochrome CycA1
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-
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additional information
?
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Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
O33823
direct interaction between rusticyanin and Cyc2, but no interaction between Cyc2 and c4-type cytochrome Cyc1 or c4-type cytochrome CycA1
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
rusticyanin
Rus, need for rusticyanin in the anaerobic electron transport pathway
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
cells grown anaerobically on S0 as an electron donor and Fe3+ as an electron acceptor, gene transcript profile of gene cyc2 monitored throughout the cells' growth phases. Reduction in the abundance of Cyc2 in anaerobic cells
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
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cells grown anaerobically on S0 as an electron donor and Fe3+ as an electron acceptor, gene transcript profile of gene cyc2 monitored throughout the cells' growth phases. Reduction in the abundance of Cyc2 in anaerobic cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the cytochrome c Cyc2 is outer membrane-bound
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partially purified by ammonium sulfate precipitation and SP-Sephadex C-25 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene cyc2, genetic organization, quantitative real-time PCR gene expression analysis
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gene cyc2, the gene is encoded in the iron oxidation system-encoding rus operon comprising genes cyc1, cyc2, coxA, coxC and rus, quantitative real-time PCR gene expression analysis in strain CCM 4253
recombinant plasmid pTCYC2 containing cyc2 gene under the control of Ptac promoter is constructed and transferred into Acidithiobacillus ferrooxidans ATCC19859
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
quantitative 2D-PAGE proteomic analysis of a resting cell suspension of a sulfur-grown Acidithiobacillus ferrooxidans CCM 4253 subculture that has lost its iron-reducing activity reveals that 147 protein spots are downregulated relative to an iron-reducing resting cell suspension of the antecedent sulfur-oxidizing culture and 111 are upregulated. Gene cyc2 encoding the enzyme is strongly downregulated
quantitative 2D-PAGE proteomic analysis of a resting cell suspension of a sulfur-grown Acidithiobacillus ferrooxidans CCM 4253 subculture that has lost its iron-reducing activity reveals that 147 protein spots are downregulated relative to an iron-reducing resting cell suspension of the antecedent sulfur-oxidizing culture and 111 are upregulated. Gene cyc2 encoding the enzyme is strongly downregulated
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quantitative 2D-PAGE proteomic analysis of a resting cell suspension of a sulfur-grown Acidithiobacillus ferrooxidans CCM 4253 subculture that has lost its iron-reducing activity reveals that 147 protein spots are downregulated relative to an iron-reducing resting cell suspension of the antecedent sulfur-oxidizing culture and 111 are upregulated. Gene cyc2 encoding the enzyme is strongly downregulated
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
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LINKS TO OTHER DATABASES (specific for EC-Number 1.16.9.1)
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