Low temperature photolysis of denatured nitrosyl hemoproteins.
Photolysis of denatured HbNO were carried out at temperatures below 26 K. The normalized kinetic curves were fitted using either two exponentials or a conformational substate energy distribution or a fractal model. The parameters are related to the protein structure. The two exponentials model assumes the existence of two fractions of photolysed molecules that rebind with slow and fast reaction rates. Only the slow reaction rate is sensitive to the denaturation process. The pre-exponential factor and the peak energy of the substate distribution values suggest an increase in the entropy and a decrease of the flexibility in the denatured samples, respectively. The fractal model parameters strengthened the functional relevance of the flexibility of the protein chain.
Alves
O C
OC
Universidade Federal Flumininse, Niteroi/RJ, Brazil.
Wajnberg
E
E
D004578:Electron Spin Resonance Spectroscopy; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D009569:Nitric Oxide / Q000737:chemistry; D010782:Photolysis; D011489:Protein Denaturation; D013329:Structure-Activity Relationship; D013696:Temperature
D006454:Hemoglobins; D009569:Nitric Oxide