Spectroscopic Studies for Rhodium (III) Binding to Apo-Transferrin

Figure 5

Curve fitting analysis of amide I (1700-1600 cm^-1) of (a) ApoHST with no Rh(III) – α-helix 53%, β-sheet 23%, β-turns 10%, and β-antiparallel 14%; (b) Rh (III)-ApoHST 0.25 mM, ApoHST:Rh (III) =1 : 0.5 - α-helix 49%, β-sheet 32%, β-turns 13%, and β-antiparallel 6%; (c) Rh (III)-ApoHST 0.5 mM, ApoHST:Rh (III) =1 : 1 - α-helix 42%, β-sheet 41%, β-turns 11%, and β-antiparallel 6%; (d) Rh (III)-ApoHST 1 mM, ApoHST:Rh (III) =1 : 2 - α-helix 39%, β-sheet 43%, β-turns 12%, and β-antiparallel 6%. The bonding interaction was performed in tris buffer at physiological pH.

(a)

(b)

(c)

(d)