[The conformational dynamic of the tetramer hemoglobin molecule as revealed by hydrogen exchange. II. Influence of the intersubunit contact splitting].
The rate of the H-D exchange of the peptide NH atoms of the isolated alpha and beta subunits of human Hb were studied at the pH range 5.5-9.0 and 20 degrees C by the IR spectroscopy. The factor retardation of the exchange rate of subunits -P in the range -10(2)-10(7). In comparison with tetramer Hb the probability of local fluctuations (1/P) is increased to a slightly greater extent for the monomeric alpha subunits then for the tetramer beta subunits. Unlike Hb oxygenation of subunits does not influence on the probability of the local fluctuations and subunits have no the pH-dependent change of the value 1/P observable for the ligand Hb. The possible mechanisms of the overall intensification of the local fluctuations upon the splitting of the Hb tetrameric contacts between subunits are discussed with the inviting of the structural crystallographic data.
Abaturov
L V
LV
Molchanova
T P
TP
Nosova
N G
NG
Shliapnikov
S V
SV
Faĭzulin
D A
DA
D000818:Animals; D020134:Catalytic Domain; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D006859:Hydrogen / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D020836:Protein Structure, Quaternary; D013055:Spectrophotometry, Infrared; D050661:Sperm Whale
D006454:Hemoglobins; D006859:Hydrogen