Long-Range Effects in Liganded Hemoglobin Investigated by Neutron and UV Raman Scattering, FTIR, and CD Spectroscopies

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• 作者：Olivier Sire ; Christian Zentz ; Serge Pin ; Laurent Chinsky ; Pierre-Yves Turpin ; Pierre Martel ; Patrick T. T. Wong ; and Bernard Alpert
• 刊名：Journal of the American Chemical Society
• 出版年：1997
• 出版时间：December 17, 1997
• 年：1997
• 卷：119
• 期：50
• 页码：12095 - 12099
• 全文大小：322K
• 年卷期：v.119,no.50(December 17, 1997)
• ISSN：1520-5126

文摘

The numerous investigations that have focused on theiron binding site to explain the different affinity ofhemoglobin for CO and O₂ are still without success.Thus, this work addresses the problem of nonlocaleffects,which have been disregarded so far. We have investigated theprotein behavior in relation to the iron-ligand nature.The present data show that different parts of the protein, whichare not in close contact with the heme pocket, areeffectively influenced by the nature of the iron-ligand bond.Whereas oxyhemoglobin and carbonmonoxidehemoglobin in solution exhibit the same molecular shapes and helicalcontents, different electrostatic interactions inassociation with a redistribution of the strains occur in the proteinmatrix. Due to electric couplings of the heme tothe protein, the whole molecule is sensitive to the chemical nature ofthe iron-ligand bond. This suggests that longdistance electrostatic interactions promote the energy transductionthrough the protein molecule.