<p>Time dependent heme hydroxylation of wild type LepHO (●) and F157I mutant (○) by H<sub>2</sub>O<sub>2</sub> in aerobic conditions as monitored by increase in absorbance at 671 nm (A) or under anaerobiosis as monitored by decrease in absorbance at 403 nm.</p
In addition to heme’s role as the prosthetic group buried inside many different proteins that are ub...
It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may b...
AbstractUsing radiolysis with 32P enriched phosphate as an internal source of ionizing radiation, th...
<p>Time dependent formation (A) and autoxidation (B) of the ferrous heme complex of wild type LepHO ...
Mutation of His-39, one of the axial ligands in rat outer mitochondrial membrane cytochrome b5 (OM c...
Free radical formation in heme proteins is recognised as a factor in mediating the toxicity of perox...
Heme Oxygenase (HO), a heme-degrading enzyme, is responsible for many physiological functions includ...
Heme is a highly abundant prosthetic group of proteins, which are involved in oxygen transport and r...
Electronic changes of iron- and metal free porphyrins are reviewed in light of their importance to m...
<p>(A): 10 mM final concentration of ascorbate was added to the HemS-heme complex (10 µM). The spect...
Slow heme transfer from horseradish peroxidases C2 and A2, cytochrome c peroxidase, chloroperoxidase...
<p>(A) Kinetics of the conversion of protoporphyrin IX into heme <i>b</i> by HemH. Varying concentra...
The autoxidation of hemoglobin was markedly increased when the solution of hemoglobin was irradiated...
The selective oxidation of the α-position of two heme-Fe<sup>III</sup> tetraarylporphryinate complex...
<p>The rate of LDL oxidation was traced in reaction mixtures containing either Hb or Mb (3 µM), LDL ...
In addition to heme’s role as the prosthetic group buried inside many different proteins that are ub...
It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may b...
AbstractUsing radiolysis with 32P enriched phosphate as an internal source of ionizing radiation, th...
<p>Time dependent formation (A) and autoxidation (B) of the ferrous heme complex of wild type LepHO ...
Mutation of His-39, one of the axial ligands in rat outer mitochondrial membrane cytochrome b5 (OM c...
Free radical formation in heme proteins is recognised as a factor in mediating the toxicity of perox...
Heme Oxygenase (HO), a heme-degrading enzyme, is responsible for many physiological functions includ...
Heme is a highly abundant prosthetic group of proteins, which are involved in oxygen transport and r...
Electronic changes of iron- and metal free porphyrins are reviewed in light of their importance to m...
<p>(A): 10 mM final concentration of ascorbate was added to the HemS-heme complex (10 µM). The spect...
Slow heme transfer from horseradish peroxidases C2 and A2, cytochrome c peroxidase, chloroperoxidase...
<p>(A) Kinetics of the conversion of protoporphyrin IX into heme <i>b</i> by HemH. Varying concentra...
The autoxidation of hemoglobin was markedly increased when the solution of hemoglobin was irradiated...
The selective oxidation of the α-position of two heme-Fe<sup>III</sup> tetraarylporphryinate complex...
<p>The rate of LDL oxidation was traced in reaction mixtures containing either Hb or Mb (3 µM), LDL ...
In addition to heme’s role as the prosthetic group buried inside many different proteins that are ub...
It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may b...
AbstractUsing radiolysis with 32P enriched phosphate as an internal source of ionizing radiation, th...