User:JJMercado21/Rubrerythrin
![](http://upload.wikimedia.org/wikipedia/commons/thumb/a/ad/PDB_1nnq_EBI.jpg/220px-PDB_1nnq_EBI.jpg)
Rubrerythrin(RBR) is a non-heme iron-containing metalloprotein involved in oxidative stress tolerance within anaerobic bacteria.[1] It contains a di-iron active site, where peroxide is reduced into two water molecules, and a mono-iron rubredoxin-like domain thought to be involved in electron transfer.[2] A majority of known RBR families are utilized as peroxide "scavengers" to defend organisms against oxidative stress.
![]() | This is the sandbox page where you will draft your initial Wikipedia contribution.
If you're starting a new article, you can develop it here until it's ready to go live. If you're working on improvements to an existing article, copy only one section at a time of the article to this sandbox to work on, and be sure to use an edit summary linking to the article you copied from. Do not copy over the entire article. You can find additional instructions here. Remember to save your work regularly using the "Publish page" button. (It just means 'save'; it will still be in the sandbox.) You can add bold formatting to your additions to differentiate them from existing content. |
Function
[edit]As a member of the Ferritin-like superfamily, RBRs primary function is iron storage and detoxification. Rubrerythrins utilize their di-iron centers to bind with reactive oxygen species such as Hydrogen Peroxide, further reducing them into water.
RBR reduction is theorized as a particularly important adaptation that occurred in response to the Great Oxygenation event, increasing defensive fitness of all cells exposed to relatively high levels of oxygen and similar byproducts.[3]
Although primarily studied within anaerobic bacteria, RBRs have been discovered in multiple different types of cells including: Aerobic, Anaerobic, and Cyanobacteria.[4]
Structure
[edit]Many formations of RBRs can be identified by four helical structures, chains alpha and beta containing 3 iron atoms. Both N and C-terminals of common RBRs are very similar to Rubredoxin containing amino acid residue sequences. Furthermore, both metalloproteins contain 5 histidine ligands located within the N-terminals of their peptide chains.[5]
Mechanism
[edit]In a reduced state without exposure to reactive oxygen byproducts, Rubrerythrin contains two water molecules near its di-iron center. During and after exposure to peroxide, Rubrerythrin becomes oxidized, changing rotational conformations beginning around the peroxide binding site.[6]
References
[edit]- ^ Sztukowska, Maryta; Bugno, Marcin; Potempa, Jan; Travis, James; Kurtz Jr, Donald M. (2002-04-25). "Role of rubrerythrin in the oxidative stress response of Porphyromonas gingivalis". Molecular Microbiology. 44 (2): 479–488. doi:10.1046/j.1365-2958.2002.02892.x. ISSN 0950-382X.
- ^ deMaré, Fredrick; Kurtz, Donald M.; Nordlund, Pär (1996-06). "The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains". Nature Structural & Molecular Biology. 3 (6): 539–546. doi:10.1038/nsb0696-539. ISSN 1545-9993.
{{cite journal}}
: Check date values in:|date=
(help) - ^ Cardenas, Juan P.; Quatrini, Raquel; Holmes, David S. (2016-11-18). "Aerobic Lineage of the Oxidative Stress Response Protein Rubrerythrin Emerged in an Ancient Microaerobic, (Hyper)Thermophilic Environment". Frontiers in Microbiology. 7. doi:10.3389/fmicb.2016.01822. ISSN 1664-302X.
{{cite journal}}
: CS1 maint: unflagged free DOI (link) - ^ Weinberg, Michael V.; Jenney, Francis E.; Cui, Xiaoyuan; Adams, Michael W. W. (2004-12). "Rubrerythrin from the Hyperthermophilic Archaeon Pyrococcus furiosus Is a Rubredoxin-Dependent, Iron-Containing Peroxidase". Journal of Bacteriology. 186 (23): 7888–7895. doi:10.1128/jb.186.23.7888-7895.2004. ISSN 0021-9193.
{{cite journal}}
: Check date values in:|date=
(help); line feed character in|title=
at position 49 (help) - ^ Van Beeumen, J.J.; Van Driessche, G.; Liu, M.Y.; LeGall, J. (1991-11). "The primary structure of rubrerythrin, a protein with inorganic pyrophosphatase activity from Desulfovibrio vulgaris. Comparison with hemerythrin and rubredoxin". Journal of Biological Chemistry. 266 (31): 20645–20653. doi:10.1016/s0021-9258(18)54757-8. ISSN 0021-9258.
{{cite journal}}
: Check date values in:|date=
(help) - ^ Dillard, Bret D.; Demick, Jonathan M.; Adams, Michael W. W.; Lanzilotta, William N. (2011-06-07). "A cryo-crystallographic time course for peroxide reduction by rubrerythrin from Pyrococcus furiosus". JBIC Journal of Biological Inorganic Chemistry. 16 (6): 949–959. doi:10.1007/s00775-011-0795-6. ISSN 0949-8257.