Kinetics of binding of carbon monoxide to lumbricus erythrocruorin: a possible model.
This paper represents a kinetic study of the binding of carbon monoxide by Lumbricus erythrocruorin. Observations on the quantum 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.
D000818:Animals; D001665:Binding Sites; D002248:Carbon Monoxide / Q000378:metabolism*; D006420:Hemeproteins / Q000378:metabolism*; D007700:Kinetics; D008027:Light; D009835:Oligochaeta / Q000378:metabolism*
D006420:Hemeproteins; D002248:Carbon Monoxide