Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9882184 | Archives of Biochemistry and Biophysics | 2005 | 8 Pages |
Abstract
The protein Mop from Haemophilus influenzae is a member of the molbindin family of proteins. Using isothermal titration calorimetry (ITC), Mop was observed to bind molybdate at two distinct sites with a stoichiometry of 8 mol molybdate per Mop hexamer. Six moles of molybdate bound endothermically at high affinity sites (Ka = 8.5 Ã 107 Mâ1), while 2 mol of molybdate bound exothermically at lower affinity sites (Ka = 3.7 Ã 107 Mâ1). Sulphate was also found to bind weakly at the higher affinity sites. ITC revealed that the affinity of molybdate binding to the endothermic site decreased with increasing pH and was accompanied by the transfer from the buffer to the protein of one proton per Mop monomer. These kinetic and thermodynamic results are interpreted with reference to molbindin crystal structures and data concerning molbindin binding affinities. Mop binds molybdate with high specificity, capacity, and affinity which indicates that Mop has a role as an intracellular molybdate binding protein involved in oxyanion homeostasis.
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Authors
Seth L. Masters, Geoffrey J. Howlett, Richard N. Pau,