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Information on EC 1.16.9.1 - iron:rusticyanin reductase
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1.16.9.1 iron:rusticyanin reductaseIUBMB Comments
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 7.1.1.9).
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Word Map
- 1.16.9.1
-
desulfovibrio
- vulgaris
- hildenborough
- hemes
- ferrooxidans
-
thiobacillus
- shewanella
-
holoproteins
-
ferrous
- hydrogenase
- desulfuricans
-
high-spin
- oneidensis
-
c4-type
- miyazaki
-
low-spin
- epr
The expected taxonomic range for this enzyme is: Acidithiobacillus ferrooxidans
Reaction Schemes
+
rusticyanin
=
+
reduced rusticyanin
Synonyms
Cyc2, high molecular weight c-type cytochrome, high-molecular-mass cytochrome c, high-molecular-mass monohaem cytochrome c, high-molecular-weight cytochrome c, Hmc, iron:rusticyanin oxidoreductase, outer-membrane iron oxidase, terminal Fe3+ reductase, terminal ferric iron reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cyc2
high-molecular-weight cytochrome c
outer-membrane iron oxidase
terminal Fe3+ reductase
terminal ferric iron reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Fe(II) + rusticyanin = Fe(III) + reduced rusticyanin
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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 7.1.1.9).
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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
-
-
-
-
?
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
-
-
-
?
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
-
-
-
-
?
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
-
-
-
?
additional information
?
-
direct interaction between rusticyanin and Cyc2, but no interaction between Cyc2 and c4-type cytochrome Cyc1 or c4-type cytochrome CycA1
-
-
?
additional information
?
-
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 SUBSTRATE
NATURAL 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
-
-
-
?
Fe(II) + rusticyanin
Fe(III) + reduced rusticyanin
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
-
-
-
?
additional information
?
-
direct interaction between rusticyanin and Cyc2, but no interaction between Cyc2 and c4-type cytochrome Cyc1 or c4-type cytochrome CycA1
-
-
?
additional information
?
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
rusticyanin
Rus, need for rusticyanin in the anaerobic electron transport pathway
-
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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
brenda
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
strain CCM 4253 shows 100% identity to type strain ATCC 23270
UniProt
brenda
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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
brenda
Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270
-
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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the cytochrome c Cyc2 is outer membrane-bound
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
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
-
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)
malfunction
-
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
-
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)
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
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
-
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
-
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
physiological function
-
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
-
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Appia-Ayme, C.; Guiliani, N.; Ratouchniak, J.; Bonnefoy, V.
Characterization of an operon encoding two c-type cytochromes, an aa3-type cytochrome oxidase, and rusticyanin in Thiobacillus ferrooxidans ATCC 33020
Appl. Environ. Microbiol.
65
4781-4787
1999
Acidithiobacillus ferrooxidans (O33823), Acidithiobacillus ferrooxidans
brenda
Blake, R.C.; Shute, E.A.
Respiratory enzymes of Thiobacillus ferrooxidans. Kinetic properties of an acid-stable iron:rusticyanin oxidoreductase
Biochemistry
33
9220-9228
1994
Acidithiobacillus ferrooxidans
brenda
Appia-Ayme, C.; Bengrine, A.; Cavazza, C.; Giudici-Orticoni, M.; Bruschi, M.; Chippaux, M.; Bonnefoy, V.
Characterization and expression of the co-transcribed cyc1 and cyc2 genes encoding the cytochrome c4 (c552) and a high-molecular-mass cytochrome c from Thiobacillus ferrooxidans ATCC 33020
FEMS Microbiol. Lett.
167
171-177
1998
Acidithiobacillus ferrooxidans
brenda
Yarzabal, A.; Brasseur, G.; Ratouchniak, J.; Lund, K.; Lemesle-Meunier, D.; Demoss, J.; Bonnefoy, V.
The high-molecular-weight cytochrome c Cyc2 of Acidithiobacillus ferrooxidans is an outer membrane protein
J. Bacteriol.
184
313-317
2002
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans ATCC 33020
brenda
Castelle, C.; Guiral, M.; Malarte, G.; Ledgham, F.; Leroy, G.; Brugna, M.; Giudici-Orticoni, M.
A new iron-oxidizing/O2-reducing supercomplex spanning both inner and outer membranes, isolated from the extreme acidophile Acidithiobacillus ferrooxidans
J. Biol. Chem.
283
25803-25811
2008
Acidithiobacillus ferrooxidans
brenda
Liu, W.; Lin, J.; Pang, X.; Mi, S.; Cui, S.; Lin, J.
Increases of ferrous iron oxidation activity and arsenic stressed cell growth by overexpression of Cyc2 in Acidithiobacillus ferrooxidans ATCC19859
Biotechnol. Appl. Biochem.
60
623-628
2013
Acidithiobacillus ferrooxidans
brenda
Kucera, J.; Pakostova, E.; Lochman, J.; Janiczek, O.; Mandl, M.
Are there multiple mechanisms of anaerobic sulfur oxidation with ferric iron in c?
Res. Microbiol.
167
357-366
2016
Acidithiobacillus ferrooxidans (O33823), Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270 (O33823)
brenda
Kucera, J.; Sedo, O.; Potesil, D.; Janiczek, O.; Zdrahal, Z.; Mandl, M.
Comparative proteomic analysis of sulfur-oxidizing Acidithiobacillus ferrooxidans CCM 4253 cultures having lost the ability to couple anaerobic elemental sulfur oxidation with ferric iron reduction
Res. Microbiol.
167
587-594
2016
Acidithiobacillus ferrooxidans (O33823), Acidithiobacillus ferrooxidans CCM 4253 / ATCC 23270 (O33823)
brenda
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