Organism | UniProt | Comment | Textmining |
---|---|---|---|
Shewanella frigidimarina | - |
NCIMB400 | - |
Shewanella frigidimarina NCIMB400 | - |
NCIMB400 | - |
Shewanella oneidensis | - |
MR-1 | - |
Shewanella oneidensis MR-1 / ATCC 700550 | - |
MR-1 | - |
Synonyms | Comment | Organism |
---|---|---|
fumarate reductase | - |
Shewanella oneidensis |
fumarate reductase | - |
Shewanella frigidimarina |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV | Shewanella oneidensis | |
FAD | proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV | Shewanella frigidimarina | |
heme | proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV | Shewanella oneidensis | |
heme | proteins displays two redox active domains, one containing four c-type hemes (I-IV) and another containing FAD at the catalytic site. Redox titrations followed by NMR and visible spectroscopies are applied to investigate the properties that allow a chain of single-electron co-factors to sustain the activity of a multielectron catalytic site. The results show that the redox behaviour of fumarate reductases is dominated by a strong interaction between hemes II and III. This interaction facilitates a sequential transfer of two electrons from the heme domain to FAD via heme IV | Shewanella frigidimarina |