<p>In presence of peroxide, ferrous RH are oxidized to their ferric (Fe<sup>III</sup>) and/or ferryl (Fe<sup>IV</sup>) forms. Upper: Hp binds Hb (ferrous and/or ferric) thereby preventing its release. Lower: Mb heme is retained attached to globin following oxidation in a peroxidase-like form. However, binding of CO to ferrous Mb prevents its oxidation to a ‘peroxidase-like form”.</p
The adverse effects of extra-erythrocytic hemoglobin (Hb) are counterbalanced by several plasma prot...
We discuss the bonding of O_2 to hemoglobin (Hb) at the molecular level. The ideas presented here ar...
It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may b...
<p>In presence of peroxide, ferrous RH are oxidized to their ferric (Fe<sup>III</sup>) and/or ferryl...
Free radical formation in heme proteins is recognised as a factor in mediating the toxicity of perox...
In the presence of excess hydrogen peroxide (H2O2), ferrous (Fe(+2)) human hemoglobin (Hb) (α2β2) un...
Aim: Hemoglobin (Hb) becomes toxic when released from the erythrocyte. The acute phase protein hapto...
Mutation of His-39, one of the axial ligands in rat outer mitochondrial membrane cytochrome b5 (OM c...
Covalent hemoglobin binding to membranes leads to band 3 (AE1) clustering and the removal of erythro...
Hydroxylamine (HA) is an oxidant of ferrous globins and its action has been reported to be inhibited...
It is in the ferrous form that myoglobin or hemoglobin can bind molecular oxygen reversibly and carr...
The dimeric hemoglobin isolated from Scapharca inaequivalvis, HbI, is notable for its highly coopera...
Haptoglobin (Hp) is an abundant and conserved plasma glycoprotein, which binds acellular adult hemog...
Hemoglobin (Hb) inside and outside the red blood cells (RBCs) undergoes constant transformation to a...
Hemes are common elements of biological redox cofactor chains involved in rapid electron transfer. W...
The adverse effects of extra-erythrocytic hemoglobin (Hb) are counterbalanced by several plasma prot...
We discuss the bonding of O_2 to hemoglobin (Hb) at the molecular level. The ideas presented here ar...
It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may b...
<p>In presence of peroxide, ferrous RH are oxidized to their ferric (Fe<sup>III</sup>) and/or ferryl...
Free radical formation in heme proteins is recognised as a factor in mediating the toxicity of perox...
In the presence of excess hydrogen peroxide (H2O2), ferrous (Fe(+2)) human hemoglobin (Hb) (α2β2) un...
Aim: Hemoglobin (Hb) becomes toxic when released from the erythrocyte. The acute phase protein hapto...
Mutation of His-39, one of the axial ligands in rat outer mitochondrial membrane cytochrome b5 (OM c...
Covalent hemoglobin binding to membranes leads to band 3 (AE1) clustering and the removal of erythro...
Hydroxylamine (HA) is an oxidant of ferrous globins and its action has been reported to be inhibited...
It is in the ferrous form that myoglobin or hemoglobin can bind molecular oxygen reversibly and carr...
The dimeric hemoglobin isolated from Scapharca inaequivalvis, HbI, is notable for its highly coopera...
Haptoglobin (Hp) is an abundant and conserved plasma glycoprotein, which binds acellular adult hemog...
Hemoglobin (Hb) inside and outside the red blood cells (RBCs) undergoes constant transformation to a...
Hemes are common elements of biological redox cofactor chains involved in rapid electron transfer. W...
The adverse effects of extra-erythrocytic hemoglobin (Hb) are counterbalanced by several plasma prot...
We discuss the bonding of O_2 to hemoglobin (Hb) at the molecular level. The ideas presented here ar...
It has been proposed that introducing tyrosine residues into human hemoglobin (e.g. βPhe41Tyr) may b...