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).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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).
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
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
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)
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)
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)
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)
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
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
the iron:rusticyanin oxidoreductase is the primary cellular oxidant of ferrous ions in the iron respiratory electron transport chain of Thiobacillus ferrooxidans
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
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
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
HOME
login
history
all enzymes
BRENDA home
History
1.16.9.1 iron:rusticyanin reductase
more
top
Information
