Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Zea mays |
Crystallization (Comment) | Organism |
---|---|
complex of maize sulfite reductase SiR and ferredoxin. A few negative residues of ferredoxin contact with a narrow area of SiR with positive electrostatic surface potential. The [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity | Zea mays |
Protein Variants | Comment | Organism |
---|---|---|
A493G | mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity | Zea mays |
A503G | mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity | Zea mays |
Arg111Q | remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme | Zea mays |
Arg114Q | remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme | Zea mays |
Arg324Q | remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme | Zea mays |
L499G | mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity | Zea mays |
L502A | mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity | Zea mays |
Lys117Q | remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme | Zea mays |
Lys582Q | remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme | Zea mays |
Lys584Q | remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme | Zea mays |
Lys66Q | remarkably lowered activity with ferredoxin as electron donor, no significant decrease with methyl viologen. Mutant absorption spectrum is comparable with wild-type enzyme | Zea mays |
P501G | mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity | Zea mays |
P541G | mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity | Zea mays |
Q504G | mutation has no significant effects on either ferredoxin-dependent or methyl viologen-dependent activity | Zea mays |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | O23813 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
hydrogen sulfide + oxidized ferredoxin + H2O | - |
Zea mays | sulfite + reduced ferredoxin + H+ | - |
? | |
hydrogen sulfide + oxidized methyl viologen + H2O | - |
Zea mays | sulfite + reduced methyl viologen + H+ | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
[4Fe-4S]-center | in cocrystals, the [2Fe-2S] cluster of ferredoxin and the [4Fe-4S] cluster of SiR are in a close proximity | Zea mays |