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IUBMB CommentsContains 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).
Synonyms
high-molecular-weight cytochrome c, iron:rusticyanin oxidoreductase, terminal fe3+ reductase, high-molecular-mass monohaem cytochrome c, terminal ferric iron reductase, high molecular weight c-type cytochrome,
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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
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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
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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
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
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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
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metabolism
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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
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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
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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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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