Active site conformation in the αh87G mutant hemoglobin: An optical absorption and FTIR study

Valeria Militello, Maurizio Leone, Clara Fronticelli, Antonio Cupane

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

We have studied the active site conformation in the carbonmonoxy derivative of the αH87G mutant hemoglobin by means of optical absorption and FTIR spectroscopies. A red shift (â% 30 cm-1) of the Soret band peak frequency, together with a concomitant red shift (â% 2 cm-1) of the bound CO stretching frequency has been observed for the mutant protein. This indicates an altered electrostatic environment of the heme group in the mutated subunits. In view of the FTIR data showing that the bound CO molecule experiences an increased positive electrostatic field, we attribute the observed effects to a closer interaction of the CO ligand with the partially positively charged imidazole side chain of the proximal histidine.

Original languageEnglish (US)
Title of host publicationNuclear And Condensed Matter Physics
Subtitle of host publicationVI Regional Conference
PublisherAmerican Institute of Physics Inc.
Pages174-177
Number of pages4
Volume513
ISBN (Electronic)1563969297
DOIs
StatePublished - Apr 7 2000
Externally publishedYes
Event6th Regional Conference on Nuclear and Condensed Matter Physics - Palermo, Italy
Duration: Oct 14 1999Oct 15 1999

Other

Other6th Regional Conference on Nuclear and Condensed Matter Physics
CountryItaly
CityPalermo
Period10/14/9910/15/99

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ASJC Scopus subject areas

  • Physics and Astronomy(all)

Cite this

Militello, V., Leone, M., Fronticelli, C., & Cupane, A. (2000). Active site conformation in the αh87G mutant hemoglobin: An optical absorption and FTIR study. In Nuclear And Condensed Matter Physics: VI Regional Conference (Vol. 513, pp. 174-177). American Institute of Physics Inc.. https://doi.org/10.1063/1.1303356