Based on spectral analysis of solutions of aromatic, heterocyclic, and sulfur-containing amino acids, we propose an additive model and assess the roles of the studied types of amino acid residues in formation of the overall absorption spectrum of hemoglobin. We have established that the identified absorption maxima (transitions) at 243.4, 248.4, 253.2, 258.8, 261.6, 264.8, and 268.4 nm belong to phenylalanine amino acid residues. Probably the latter also form the unassigned transition at 241.0 nm. The transitions at 272.8, 274.6, 280.0, and 284.4 nm are a superposition of the absorption by the side groups of tyrosine and tryptophan; the transition at 278.2 nm is associated with tyrosine, masked by adjacent transitions of tryptophan, and the transition at 291.2 nm belongs to tryptophan. We consider the possibility of estimating the changes in the spectral properties of proteins under the influence of various physical and chemical factors using data from additive spectra.
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Translated from Zhurnal Prikladnoi Spektroskopii, Vol. 80, No. 6, pp. 907–912, November–December, 2013.
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Lavrinenko, I.A., Vashanov, G.A. & Ruban, M.K. Analysis of the Contribution of Chromophores in Side Groups of Amino Acids to the Absorption Spectrum of Hemoglobin. J Appl Spectrosc 80, 899–904 (2014). https://doi.org/10.1007/s10812-014-9862-4
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DOI: https://doi.org/10.1007/s10812-014-9862-4