We have studied the reaction of ferricytochrome c, methemoglobin and metmyoglobin with OH and alcohol radicals (methanol, ethanol, ethylene glycol and glycerol). These radicals can be divided into three groups: 1. 1.|The OH radicals which reduce the ferricytochrome c with a yield of (30 ± 10)% and methemoglobin with a yield of (40 ± 10)%. They do not reduce metmyoglobin. The reduction is not a normal bimolecular reaction but is most probably an intramolecular electron transfer of a protein radical. 2. 2.|Methanol and ethanol radicals which reduce all three hemoproteins with a yield of (100 ± 5)%. This reduction is a normal bimolecular reaction. 3. 3.|Glycerol radicals which do not reduce the ferrihemoproteins under our experimenta...
Ferricytochrome CL isolated from Hyphomicrobium X is an electron acceptor in assays for homologous m...
The electroreduction f ferr iheme was investigated by control led potential coulometry, polarography...
The reconstitution of apomyoglobin with 1.6 equivalent of Co(II)complexes of N_A-and N_B-ethylmesopo...
We have studied the reaction of ferricytochrome c, methemoglobin and metmyoglobin with OH and alcoho...
The reactions of the hydroxyalkyl radicals CH2OH and (CH3), COH with oxidized cytochrome c are far m...
The final step in the erythrocyte methemoglobin reduction pathway, the transfer of an electron from ...
By amking 1-ascorbic acid and molecular oxygens act upon methemoglobin the author studied the decomp...
Metmyoglobin (MbFe III ) from horse heart forms an oxyferryl heme (Fe IV = O) and an unstable protei...
Two-equivalent oxidation of metmyoglobin (MbIII) by hydrogen peroxide (H2O2) yields an oxoferryl moi...
Earlier studies have clarified that NADH and NADPH, re-energized repeatedly by red blood cell (RBC) ...
1. 1. The reaction of hydrated electrons with ferricytochrome c was studied using the pulse-radiolys...
ABSTRACT: Microsomes and reconstituted systems containing cytochrome P450 can oxidize glycerol to fo...
AbstractThe interaction of ascorbate with different heme iron redox states of myoglobin (ferrylmyogl...
An assay for determining the rate of methemoglobin reduction in hemolysates of human erythrocytes ha...
Metmyoglobin (MbFeIII), a major form of dietary iron, is an efficient inducer of lipid and protein o...
Ferricytochrome CL isolated from Hyphomicrobium X is an electron acceptor in assays for homologous m...
The electroreduction f ferr iheme was investigated by control led potential coulometry, polarography...
The reconstitution of apomyoglobin with 1.6 equivalent of Co(II)complexes of N_A-and N_B-ethylmesopo...
We have studied the reaction of ferricytochrome c, methemoglobin and metmyoglobin with OH and alcoho...
The reactions of the hydroxyalkyl radicals CH2OH and (CH3), COH with oxidized cytochrome c are far m...
The final step in the erythrocyte methemoglobin reduction pathway, the transfer of an electron from ...
By amking 1-ascorbic acid and molecular oxygens act upon methemoglobin the author studied the decomp...
Metmyoglobin (MbFe III ) from horse heart forms an oxyferryl heme (Fe IV = O) and an unstable protei...
Two-equivalent oxidation of metmyoglobin (MbIII) by hydrogen peroxide (H2O2) yields an oxoferryl moi...
Earlier studies have clarified that NADH and NADPH, re-energized repeatedly by red blood cell (RBC) ...
1. 1. The reaction of hydrated electrons with ferricytochrome c was studied using the pulse-radiolys...
ABSTRACT: Microsomes and reconstituted systems containing cytochrome P450 can oxidize glycerol to fo...
AbstractThe interaction of ascorbate with different heme iron redox states of myoglobin (ferrylmyogl...
An assay for determining the rate of methemoglobin reduction in hemolysates of human erythrocytes ha...
Metmyoglobin (MbFeIII), a major form of dietary iron, is an efficient inducer of lipid and protein o...
Ferricytochrome CL isolated from Hyphomicrobium X is an electron acceptor in assays for homologous m...
The electroreduction f ferr iheme was investigated by control led potential coulometry, polarography...
The reconstitution of apomyoglobin with 1.6 equivalent of Co(II)complexes of N_A-and N_B-ethylmesopo...