Pulse radiolytic investigation of single heme group reduction in hum an methemoglobin.
Reduction of one of the four heme groups of human aquomethemoglobin A has been investigated by the pulse radiolysis method. The reactivity of e-a-q, the hydrated electron, with methemoglobin was determined by observing this species directly. The separate reactions of the hydroxy yl radical and hydrogen atom, as well as of e-a-q, were studied by observing absorbance changes in the protein spectrum over the wavelength range 290 to 600nm, with appropriate scavengers in solution...
D001386:Azides / Q000097:blood; D001665:Binding Sites; D003486:Cyanides / Q000097:blood; D004583:Electrons; D006418:Heme; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D046911:Macromolecular Substances; D008433:Mathematics; D008706:Methemoglobin; D010084:Oxidation-Reduction; D011485:Protein Binding; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D014978:Xenon
D001386:Azides; D003486:Cyanides; D046911:Macromolecular Substances; D014978:Xenon; D006418:Heme; D008706:Methemoglobin