Conformational changes and ligand dissociation kinetics following rapid reduction of human aquomethemoglobin and horse aquometmyoglobin by hydrated electrons.

Wilting, J; Raap, A; Braams, R; De Bruin, S H; Rollema, H S; Janssen, L H

Wilting, J; Raap, A; Braams, R; De Bruin, S H; Rollema, H S; Janssen, L H.

J Biol Chem ; 249(19): 6325-30, 1974 Oct 10.

Article in En | MEDLINE | ID: mdl-4423163

Subject(s)

Methemoglobin; Myoglobin; Animals; Argon; Binding Sites; Electrons; Ferricyanides; Half-Life; Horses; Humans; Hydrogen-Ion Concentration; Inositol; Iodoacetates; Iron; Kinetics; Ligands; Organophosphorus Compounds; Oxidation-Reduction; Oxyhemoglobins; Protein Binding; Protein Conformation; Species Specificity; Spectrophotometry; Sulfhydryl Compounds; Time Factors

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Collection: 01-internacional Database: MEDLINE Main subject: Methemoglobin / Myoglobin Limits: Animals / Humans Language: En Journal: J Biol Chem Year: 1974 Document type: Article Country of publication: United States

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