Temperature Dependent Soret Spectral Band Shifts Accompany Human CN-Mesohemoglobin Assembly |
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Authors: | Priyani V Fonseka Gayathri Vasudevan Lisa-Jo Ann Clarizia Melisenda J McDonald |
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Institution: | (1) Department of Chemistry, University of Massachusetts, Lowell, MA 01854, USA;(2) Present address: Columbus Children’s Hospital Research Institute, Columbus, OH 43054, USA;(3) Present address: Department of Chemistry, Wellesley College, Wellesley, MA, USA |
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Abstract: | The interaction between human apohemoglobin A and CN-Mesohemin, a monomeric non-native heme derivative, was probed by Soret
spectrophotometric titrations in 0.05 M potassium phosphate buffer, pH 7 at varied temperatures. Hypsochromic shifts in the
absorbance maxima were observed at all temperatures below 10°C. First derivative spectroscopy of CN-Mesohemin titrations was
used to provide further evidence of a spectral shift upon CN-Mesohemoglobin assembly. Findings of Soret Spectral shifts demonstrate
a preference for the α chain heme site by CN-Mesohemin indicative of semi-α-hemoglobin intermediate formation. CN-Mesohemin,
a derivative with peripheral 2,4 ethyl groups, does not possess the extended conjugation seen for native CN-Protohemin with
its 2,4 vinyl groups. Indeed, reduced polarity of CN-Mesohemin over that of CN-Protohemin resulted in distinct temperature
dependencies. Molecular visualization and protein-ligand interaction analysis targeted a functionally diverse residue unique to the α-chain. Tyrosine-42 (a polar/non-polar amino acid) appeared to play a prominent role in the assembly
process. |
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Keywords: | Apohemoglobin A CN-Mesohemin protein– ligand interactions Soret region |
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