Kinetics of carbon monoxide and oxygen binding for eight electrophoretic components of sperm-whale myoglobin

Biochemistry ◽  
1972 ◽  
Vol 11 (24) ◽  
pp. 4520-4525 ◽  
Author(s):  
Joyce LaGow ◽  
Lawrence J. Parkhurst
Keyword(s):  
Carbon Monoxide ◽  
Sperm Whale ◽  
Oxygen Binding ◽  
Kinetics Of ◽  
Sperm Whale Myoglobin

scholarly journals Extended Molecular Dynamics Simulation of the Carbon Monoxide Migration in Sperm Whale Myoglobin

2004 ◽  
Vol 86 (6) ◽  
pp. 3855-3862 ◽  
Author(s):  
Cecilia Bossa ◽  
Massimiliano Anselmi ◽  
Danilo Roccatano ◽  
Andrea Amadei ◽  
Beatrice Vallone ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Carbon Monoxide ◽  
Molecular Dynamics Simulation ◽  
Sperm Whale ◽  
Dynamics Simulation ◽  
Sperm Whale Myoglobin

scholarly journals Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins

1987 ◽  
Vol 243 (1) ◽  
pp. 205-210 ◽  
Author(s):  
H S Aojula ◽  
M T Wilson ◽  
I E G Morrison
Keyword(s):  
Ligand Binding ◽  
Kinetic Parameters ◽  
Sperm Whale ◽  
Binding Kinetics ◽  
Orientational Disorder ◽  
Binding Properties ◽  
Functional Consequences ◽  
Kinetics Of ◽  
Sperm Whale Myoglobin ◽  
O2 Dissociation

Ligand-binding kinetics of native and reconstituted sperm-whale myoglobin were studied in relation to haem orientational disorder by rapid kinetic methods. In addition, native yellow-fin-tuna myoglobin with significant amount of haem disorder was also used. The O2 dissociation and association rates were found for the proteins with different degrees of haem disorder, and these results suggest that the isomers are characterized by almost identical kinetic parameters. Rates of CO recombination after photolysis were also identical for the two orientational isomers. The results clearly indicate that the rotation of the haem about the alpha-gamma meso axis has little or no effect on the ligand-binding properties of these myoglobins.

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