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http://dx.doi.org/10.5483/BMBRep.2011.44.3.170

Protection of aquo/hydroxocobalamin from reduced glutathione by a B12 trafficking chaperone  

Jeong, Jin-Ju (School of Biotechnology, Yeungnam University)
Ha, Tal-Soo (Department of Biomedical Science, College of Natural Science, Daegu University)
Kim, Ji-Hoe (School of Biotechnology, Yeungnam University)
Publication Information
BMB Reports / v.44, no.3, 2011 , pp. 170-175 More about this Journal
Abstract
We identified a bovine $B_{12}$ trafficking chaperone bCblC in Bos taurus that showed 88% amino acid sequence identity with a human homologue. The protein bCblC was purified from E. coli by over-expression of the encoding gene. bCblC bound cyanocobalamin (CNCbl), methylcobalamin (MeCbl) and adenosylcobalamin (AdoCbl) in the base-off states and eliminated the upper axial ligands forming aquo/hydroxocobalamin ($OH_2$/OHCbl) under aerobic conditions. A transition of $OH_2$/OHCbl was induced upon binding to bCblC. Interestingly, bCblC-bound $OH_2$/OHCbl did not react with reduced glutathione (GSH), while the reaction of free$OH_2$/OHCbl with GSH resulted in the formation of glutathionylcobalamin (GSCbl) and glutathione disulfide (GSSG). Furthermore we found that bCblC eliminates the GSH ligand of GSCbl forming $OH_2$/OHCbl. The results demonstrated that bCblC is a $B_{12}$ trafficking chaperone that binds cobalamins and protects $OH_2$/OHCbl from GSH, which could be oxidized to GSSG by free $OH_2$/OHCbl.
Keywords
Cobalamin; Glutathione; Oxidative stress; Trafficking chaperone;
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