Abstract

Infrared absorption spectra of the α-104 (G11) cysteine SH group have been observed for aqueous solutions of hemoglobin derivatives from humans, pigs, and horses. The center frequencies (νSH) show ligand sensitive patterns that are similar for the three species, with νSH (HbCO) < νSH (HbO₂ ~ HbCN) < νSH (Hb⁺) ≪ νSH (deoxyHb) for human and pig hemoglobins. The α-104 SH group is most strongly H-bonded (smallest νSH), has the greatest range of νSH (Hb → HbCO) in human hemoglobin, and is least strongly H-bonded and has the smallest range of νSH (Hb → HbCO) in horse hemoglobin. The β-112 cysteine SH in human hemoglobin is more weakly H-bonded than is the α-104 SH. These studies illustrate how FTIR can be used to measure differences in protein structure that are related to biological control mechanisms.

© 1978 Optical Society of America

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