Protein Variants | Comment | Organism |
---|---|---|
additional information | labeling of cysteinyl residues in the active site by alkylation and spectroscopic analysis, overview | Spinacia oleracea |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Spinacia oleracea | 9507 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | nature, properties, and function of the Fe-S cluster in spinach FTR, overview. [4Fe-4S]2+ cluster covalently attached through a cluster sulfide to a cysteine-based thiyl radical formed on one of the active-site thiols, and at least partial cluster oxidation to the [4Fe-4S]3+ state. Proposed canonical structures for the Fe-S cluster in N-ethylmaleimide-modified spinach FTR, overview. Detailed spectroscopic analysis | Spinacia oleracea | |
Iron | presence of an S = 0 [4Fe-4S]2+ cluster with complete cysteinyl-S coordination that cannot be reduced at potentials down to -650 mV, but can be oxidized by ferricyanide to an S = 1/2 [4Fe-4S]3+ state. The midpoint potential for the [4Fe-4S]3+/2+ couple is estimated to be +420 mV versus NHE. Results argue against a role for the cluster in mediating electron transport from ferredoxin to the active-site disulfide and suggest an alternative role for the cluster in stabilizing the one-electron-reduced intermediate. A mechanistic scheme is proposed involving sequential one-electron redox processes with the role of the [4Fe-4S]2+ cluster being to stabilize the thiyl radical formed by the initial one-electron reduction of the active-site disulfide | Spinacia oleracea |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Spinacia oleracea | - |
- |
- |
Purification (Comment) | Organism |
---|---|
native enzyme from leaves | Spinacia oleracea |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
leaf | - |
Spinacia oleracea | - |
Synonyms | Comment | Organism |
---|---|---|
FTR | - |
Spinacia oleracea |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
4Fe-4S-center | presence of an S = 0 [4Fe-4S]2+ cluster with complete cysteinyl-S coordination that cannot be reduced at potentials down to -650 mV, but can be oxidized by ferricyanide to an S = 1/2 [4Fe-4S]3+ state. The midpoint potential for the [4Fe-4S]3+/2+ couple is estimated to be +420 mV versus NHE. Results argue against a role for the cluster in mediating electron transport from ferredoxin to the active-site disulfide and suggest an alternative role for the cluster in stabilizing the one-electron-reduced intermediate. A mechanistic scheme is proposed involving sequential one-electron redox processes with the role of the [4Fe-4S]2+ cluster being to stabilize the thiyl radical formed by the initial one-electron reduction of the active-site disulfide | Spinacia oleracea |
General Information | Comment | Organism |
---|---|---|
additional information | role for Fe-S clusters in the enzyme mechanism involving both the stabilization of a thiyl radical intermediate and cluster site-specific chemistry involving a bridging sulfide | Spinacia oleracea |