EC Number   |
General Information |
Reference |
|---|
   1.16.9.1 | 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) |
-, 746419 |
| 1.16.9.1 | malfunction |
by overexpression of Cyc2 in Acidithiobacillus ferrooxidans Fe2+ oxidation activity and arsenic stressed cell growth is increased |
727208 |
| 1.16.9.1 | 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) |
-, 746418 |
| 1.16.9.1 | 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 |
-, 746418 |
| 1.16.9.1 | 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 |
-, 746419 |
| 1.16.9.1 | 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 |
-, 746418 |
| 1.16.9.1 | physiological function |
the iron:rusticyanin oxidoreductase is the primary cellular oxidant of ferrous ions in the iron respiratory electron transport chain of Thiobacillus ferrooxidans |
714133 |
