Abstract
The interaction of apohemoglobin with two heme derivatives, CN-protohemin and CN-deuterohemin, was monitored at multiple Soret wavelengths (417–423 and 406–412 nm, respectively) in 0.05 M potassium phosphate buffer, pH 7.0, at 10°C and revealed, as previously reported, a multiphasic kinetic reaction. Wavelength-dependent reactions were observed for both CN-protohemin and CN-deuterohemin derivatives with the a chain (bathochromic entity) displaying faster (4- to 7-fold) rates throughout the courses of both heme-binding reactions. The basis of this spectrally heterogeneous kinetic phenomenon could be deduced from molecular modeling studies of α- and β-chain structures. Key differences in the number of stabilizing contacts of the two chains with the peripheral a propionyl 45(CE3); 58(E7); 61(E10) as well as the b vinyl 38(C4); 71(E15); 106(G8) groups were found. Furthermore, RMS plots comparing apo- and heme-containing subunits reveal substantial structural disparities in the C-CD-F-FG helical regions of the αβ dimer interface.
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Vasudevan, G., McDonald, M.J. Wavelength-Dependent Spectral Changes Accompany CN-Hemin Binding to Human Apohemoglobin. J Protein Chem 19, 583–590 (2000). https://doi.org/10.1023/A:1007150318854
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DOI: https://doi.org/10.1023/A:1007150318854