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. 1979 Feb;76(2):549–552. doi: 10.1073/pnas.76.2.549

Absence of heme-localized strain in T state hemoglobin: insensitivity of heme-imidazole resonance Raman frequencies to quaternary structure.

J Kincaid, P Stein, T G Spiro
PMCID: PMC382985  PMID: 284379

Abstract

Substitution of pentadeuterated 2-methylimidazole in (2-methylimidazole)-Fe(II)-protoporphyrin IX, a model complex for deoxyHb, shifts three bands in the low-frequency resonance Raman spectrum 380 leads to 373 cm-1, 348 leads to 345 cm-1, and 220 leads to 218 cm-1. The first of these is assigned primarily to Fe-imidazole stretching, and the other two are assigned to porphyrin deformation modes with substantial Fe-pyrrole stretching contributions. The three bands are observed in deoxyHb and Mb. The Fe-pyrrole modes are at essentially the same frequencies in the two proteins, but the Fe-imidazole mode is 6 cm-1 lower in deoxyHb than Mb, implying a slight alteration in the heme-imidazole linkage. No change greater than 2 cm-1 is observed when Hb Kempsey is switched from the R to the T state. This observation places an upper limit on the energy stored in the Fe-imidazole bond of T state deoxyHb, which is estimated to be less than 0.2 kcal/mol (less than 836.8 J/mol).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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