Protection of aquo/hydroxocobalamin from reduced glutathione by a B-12 trafficking chaperone

Title
Protection of aquo/hydroxocobalamin from reduced glutathione by a B-12 trafficking chaperone
Author(s)
김지회정진주[정진주]하달수[하달수]
Keywords
METHYLMALONIC ACIDURIA; METHIONINE SYNTHASE; BINDING; IDENTIFICATION; VITAMIN-B-12; GLUTATHIONYLCOBALAMIN; ADENOSYLTRANSFERASE; HOMOCYSTINURIA; COBALAMINS
Issue Date
201103
Publisher
KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
Citation
BMB REPORTS, v.44, no.3, pp.170 - 175
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 (OH2/OHCbl) under aerobic conditions. A transition of OH2/OHCbl was induced upon binding to bCblC. Interestingly, bCblC-bound OH2/OHCbl did not read with reduced glutathione (GSH), while the reaction of free OH2/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 OH2/OHCbl. The results demonstrated that bCblC is a B-12 trafficking chaperone that binds cobalamins and protects OH2/OHCbl from GSH, which could be oxidized to GSSG by free OH2/OHCbl. [BMB reports 2011; 44(3): 170-175]
URI
http://hdl.handle.net/YU.REPOSITORY/25550http://dx.doi.org/10.5483/BMBRep.2011.44.3.170
ISSN
1976-6696
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생명공학부 > 생명공학부 > Articles
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