 | This article needs additional citations for verification. (October 2017) |
| Rubredoxin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 rubredoxin domain ii from pseudomonas oleovorans | |||||||||
| Identifiers | |||||||||
| Symbol | Rubredoxin | ||||||||
| Pfam | PF00301 | ||||||||
| Pfam clan | CL0045 | ||||||||
| InterPro | IPR004039 | ||||||||
| PROSITE | PDOC00179 | ||||||||
| SCOP2 | 7rxn / SCOPe / SUPFAM | ||||||||
| |||||||||
Rubredoxins are a class of low-molecular-weight iron-containing proteins found in sulfur-metabolizing bacteria and archaea. Sometimes rubredoxins are classified as iron-sulfur proteins; however, in contrast to iron-sulfur proteins, rubredoxins do not contain inorganic sulfide. Like cytochromes, ferredoxins and Rieske proteins, rubredoxins are thought to participate in electron transfer in biological systems. Recent work in bacteria[1] and algae[2] have led to the hypothesis that some rubredoxins may instead have a role in delivering iron to metalloproteins.
- ^ Liu, F; Geng, J; Gumper, RH; Barman, A; Ozarowski, A; Hamelberg, D; Liu, A (June 2015). "An iron reservoir to the catalytic metal: The rubredoxin iron in an extradiol dioxygenase". The Journal of Biological Chemistry. 290 (25): 15621–15634. doi:10.1074/jbc.M115.650259. PMC 4505474. PMID 25918158. Retrieved 6 February 2023.
- ^ Calderon, RH; de Vitry, C; Wollman, FA; Niyogi, KK (February 2023). "Rubredoxin 1 promotes the proper folding of D1 and is not required for heme b559 assembly in Chlamydomonas photosystem II". The Journal of Biological Chemistry. 299 (3). doi:10.1016/j.jbc.2023.102968. PMC 9986647. PMID 36736898. Retrieved 6 February 2023.