3oa8

Structural highlights

Function

[SOXA_STAND] C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosulfate or other inorganic sulfur substrates. This leads to the liberation of two electrons, which may be transferred from the SoxAX complex to another cytochrome c that then channels them into the respiratory electron transport chain. Some electrons may be used for reductive CO(2) fixation.^{[1] [2] [3] [4]}

References

1. ↑ Kappler U, Aguey-Zinsou KF, Hanson GR, Bernhardt PV, McEwan AG. Cytochrome c551 from Starkeya novella: characterization, spectroscopic properties, and phylogeny of a diheme protein of the SoxAX family. J Biol Chem. 2004 Feb 20;279(8):6252-60. Epub 2003 Nov 26. PMID:14645228 doi:http://dx.doi.org/10.1074/jbc.M310644200
2. ↑ Kappler U, Hanson GR, Jones A, McEwan AG. A recombinant diheme SoxAX cytochrome - implications for the relationship between EPR signals and modified heme-ligands. FEBS Lett. 2005 Apr 25;579(11):2491-8. PMID:15848194 doi:http://dx.doi.org/10.1016/j.febslet.2005.03.060
3. ↑ Kappler U, Bernhardt PV, Kilmartin J, Riley MJ, Teschner J, McKenzie KJ, Hanson GR. SoxAX cytochromes, a new type of heme copper protein involved in bacterial energy generation from sulfur compounds. J Biol Chem. 2008 Aug 8;283(32):22206-14. doi: 10.1074/jbc.M800315200. Epub 2008 , Jun 14. PMID:18552405 doi:http://dx.doi.org/10.1074/jbc.M800315200
4. ↑ Kilmartin JR, Maher MJ, Krusong K, Noble CJ, Hanson GR, Bernhardt PV, Riley MJ, Kappler U. Insights into structure and function of the active site of SoxAX cytochromes. J Biol Chem. 2011 Jul 15;286(28):24872-81. Epub 2011 May 18. PMID:21592966 doi:http://dx.doi.org/10.1074/jbc.M110.212183