Protein Variants | Comment | Organism |
---|---|---|
E185A | CD and MCD spectra similar to wild-type | Saccharomyces cerevisiae |
E185D | 2.8 atoms of Cu per protein, CD and MCD spectra similar to wild-type | Saccharomyces cerevisiae |
Y354A | 2.8 atoms of Cu per protein, CD and MCD spectra similar to wild-type | Saccharomyces cerevisiae |
Y354F | CD and MCD spectra similar to wild-type | Saccharomyces cerevisiae |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3 | - |
hydroquinone | wild-type, pH 6.5, 25°C | Saccharomyces cerevisiae | |
3 | - |
Fe2+ | wild-type, pH 6.5, 4°C | Saccharomyces cerevisiae | |
4.6 | - |
hydroquinone | mutant Y354A, pH 6.5, 25°C | Saccharomyces cerevisiae | |
4.6 | - |
Fe2+ | mutant Y354A, pH 6.5, 4°C | Saccharomyces cerevisiae | |
8.2 | - |
hydroquinone | mutant E185D, pH 6.5, 25°C | Saccharomyces cerevisiae | |
8.2 | - |
Fe2+ | mutant E185D, pH 6.5, 4°C | Saccharomyces cerevisiae | |
12.7 | - |
hydroquinone | mutant Y354F, pH 6.5, 25°C | Saccharomyces cerevisiae | |
12.7 | - |
Fe2+ | mutant Y354F, pH 6.5, 4°C | Saccharomyces cerevisiae | |
14.1 | - |
hydroquinone | mutant E185A, pH 6.5, 25°C | Saccharomyces cerevisiae | |
14.1 | - |
Fe2+ | mutant E185A, pH 6.5, 4°C | Saccharomyces cerevisiae |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu | 4 atoms per protein | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
4 Fe(II) + 4 H+ + O2 = 4 Fe(III) + 2 H2O | iron binding site plays a major role in tuning the reduction potenzial of iron to provide a large driving force for the reaction, E185 residue provides the dominant electron transfer pathway to the T1 Cu site | Saccharomyces cerevisiae |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hydroquinone + Fe2+ + O2 | - |
Saccharomyces cerevisiae | ? | - |
? |