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Structural dynamics of myoglobin
Biophysical Chemistry, 2000Conformational fluctuations have been invoked to explain the observation that the diffusion of small ligands through a protein is a global phenomenon, as suggested (for example) by the oxygen induced fluorescence quenching of buried tryptophans. In enzymes processing large substrates, a channel to the catalytic site is often seen in the crystal ...
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2010
Hemoglobin is the vital protein that conveys oxygen from the lungs to the tissues and facilitates the return of carbon dioxide from the tissues back to the lungs [1]–[6]. Myoglobin accepts and stores the oxygen released by hemoglobin and transports it to the mitochondria. The pathways are shown in Fig. 10.1.
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Hemoglobin is the vital protein that conveys oxygen from the lungs to the tissues and facilitates the return of carbon dioxide from the tissues back to the lungs [1]–[6]. Myoglobin accepts and stores the oxygen released by hemoglobin and transports it to the mitochondria. The pathways are shown in Fig. 10.1.
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1975
The solubility of O2 in aqueous media is relatively low; one litre of pure water in equilibrium with air at 20°C and atmospheric pressure dissolves 6.59 cm3 of O293, which corresponds to a 3 × 10−4M solution. This limits the rate of diffusion of O2 from the surface of an organism and also the rate at which O2 can be delivered by a circulatory system ...
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The solubility of O2 in aqueous media is relatively low; one litre of pure water in equilibrium with air at 20°C and atmospheric pressure dissolves 6.59 cm3 of O293, which corresponds to a 3 × 10−4M solution. This limits the rate of diffusion of O2 from the surface of an organism and also the rate at which O2 can be delivered by a circulatory system ...
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On the Evolution of Myoglobin.
Systematic Zoology, 1979A. E. Romero-Herrera+4 more
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