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XANES spectroscopy of carp hemoglobin‐iron in correlation with the affinity changes of the protein for ligand
Author(s) -
Pin Serge,
Cortes Robert,
Alpert Bernard
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81043-2
Subject(s) - hemoglobin , ligand (biochemistry) , chemistry , heme , myoglobin , hemeprotein , carp , biophysics , biochemistry , crystallography , biology , receptor , enzyme , fish <actinopterygii> , fishery
The strong variation of ligand‐binding properties with pH for carp hemoglobin is not reflected in the electronic distribution of the heme‐iron. Thus, we can suppose that hemoglobin affinity is directly controlled by the protein and not by some particular changes of the iron atom.