Title : Dynamics of dioxygen and carbon monoxide binding to soybean leghemoglobin.

Pub. Date : 1985 Jul 25

PMID : 4040516






4 Functional Relationships(s)
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1 Dynamics of dioxygen and carbon monoxide binding to soybean leghemoglobin. Oxygen leghemoglobin A Glycine max
2 The association of dioxygen and carbon monoxide to soybean leghemoglobin (Lb) has been studied by laser flash photolysis at temperatures from 10 to 320 K and times from 50 ns to 100 s. Infrared spectra of the bound and the photodissociated state were investigated between 10 and 20 K. The general features of the binding process in leghemoglobin are similar to the ones found in myoglobin. Oxygen leghemoglobin A Glycine max
3 The association of dioxygen and carbon monoxide to soybean leghemoglobin (Lb) has been studied by laser flash photolysis at temperatures from 10 to 320 K and times from 50 ns to 100 s. Infrared spectra of the bound and the photodissociated state were investigated between 10 and 20 K. The general features of the binding process in leghemoglobin are similar to the ones found in myoglobin. Oxygen leghemoglobin A Glycine max
4 The association of dioxygen and carbon monoxide to soybean leghemoglobin (Lb) has been studied by laser flash photolysis at temperatures from 10 to 320 K and times from 50 ns to 100 s. Infrared spectra of the bound and the photodissociated state were investigated between 10 and 20 K. The general features of the binding process in leghemoglobin are similar to the ones found in myoglobin. Oxygen leghemoglobin A Glycine max