Open AccessImplication of the α1β1 interface in the hemoglobin affinity changes
Author(s) -
ANTRI Said EL,
ZENTZ Christian,
ALPERT Bernard
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb14535.x
Subject(s) - hemoglobin , heme , dimer , hemeprotein , cysteine , chemistry , circular dichroism , molecule , absorption (acoustics) , thiol , crystallography , infrared spectroscopy , biophysics , biochemistry , materials science , biology , organic chemistry , enzyme , composite material
The α1β1 interface of normal and mutated San Diego hemoglobins in their fully liganded form was investigated, through the SH vibrational absorption of β‐112 cysteine, byFourier‐transform infrared spectroscopy. The center frequency of this thiol group was significantly shifted in San Diego hemoglobin compared with normal human hemoglobin. Different dimer organization between the two proteins was also revealed by circular dichroism of the heme. These findings agree well with assessment that the α1β1 interface, far from being inert, is involved in the affinity changes of the hemoglobin molecule.