Function
Bacterioferritin comigratory protein or Bacterioferritin comigratory protein peroxiredoxin or Thiol peroxidase or Peroxiredoxin Q. (BCP) is part of the peroxiredoxin family of proteins. BCP is important in hydrogen peroxide resistance, nodulation and nitrogen fixation in bacteria[1]. BCP active site Cys is stabilized as a reactive cys-thiolate and attacks a bound hydrogen peroxide to form Cys-sulfenate and water[2].
Relevance
BCP has defensive role against peroxide-mediated cell killing and protects supercoiled DNA against oxidative damage[3].
Structural highlights
The BCP containing the cysteine-derivatives 3-sulfinoalanine and S-hydroxycysteine and contains 2 water molecules which mimic the oxygens of the peroxide substrate[4].
- ↑ Liu X, Qiu W, Rao B, Cao Y, Fang X, Yang J, Jiang G, Zhong Z, Zhu J. Bacterioferritin comigratory protein is important in hydrogen peroxide resistance, nodulation, and nitrogen fixation in Azorhizobium caulinodans. Arch Microbiol. 2019 Aug;201(6):823-831. doi: 10.1007/s00203-019-01654-8. Epub, 2019 Apr 5. PMID:30953092 doi:https://dx.doi.org/10.1007/s00203-019-01654-8
- ↑ Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA. Peroxiredoxin Catalysis at Atomic Resolution. Structure. 2016 Sep 1. pii: S0969-2126(16)30223-4. doi:, 10.1016/j.str.2016.07.012. PMID:27594682 doi:https://dx.doi.org/10.1016/j.str.2016.07.012
- ↑ Singh A, Kumar N, Tomar PPS, Bhose S, Ghosh DK, Roy P, Sharma AK. Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus. Protoplasma. 2017 Jul;254(4):1675-1691. doi: 10.1007/s00709-016-1062-z. Epub 2016, Dec 16. PMID:27987036 doi:https://dx.doi.org/10.1007/s00709-016-1062-z
- ↑ Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA. Peroxiredoxin Catalysis at Atomic Resolution. Structure. 2016 Sep 1. pii: S0969-2126(16)30223-4. doi:, 10.1016/j.str.2016.07.012. PMID:27594682 doi:https://dx.doi.org/10.1016/j.str.2016.07.012
