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Kinetics of Binding of Carbon Monoxide to Lumbricus Erythrocruorin: A Possible Model
G. M. Giacometti, A. Focesi, B. Giardina, M. Brunori and J. Wyman
Proceedings of the National Academy of Sciences of the United States of America
Vol. 72, No. 11 (Nov., 1975), pp. 4313-4316
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/64946
Page Count: 4
You can always find the topics here!Topics: Kinetics, Ligands, Biochemistry, Molecules, Photolysis, Luminous intensity, Carbon monoxide, Enzymes, Legends, Efficiency metrics
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This paper represents a kinetic study of the binding of carbon monoxide by Lumbricus erythrocruorin. Observations on the quantum yield and the relaxation of the system both to equilibrium and to the steady state realized in the presence of constant illumination under various conditions are reported. The results, besides indicating the existence of at least two types of binding sites, give indications as to the behavior of a complex polyfunctional molecule, such as an enzyme, working under steady-state conditions.
Proceedings of the National Academy of Sciences of the United States of America © 1975 National Academy of Sciences