Pentacoordinate respiratory hemoproteins such as hemoglobin and myoglobin have
evolved to supply cells with oxygen. However, these respiratory heme proteins are also …

The availability of genomic information from the three kingdoms of life has altered
substantially our view of the globin superfamily. It is now evident that Hbs, 2 defined as …

Significance: Failure to maintain myoglobin (Mb) in the reduced state causes the formation
of metMb, ferryl Mb species, and cross-linked Mb. Dissociation of ferriprotoporphyrin IX from …

Abstract Aim: Hemoglobin (Hb) becomes toxic when released from the erythrocyte. The
acute phase protein haptoglobin (Hp) binds avidly to Hb and decreases oxidative damage to …

Under those pathological conditions in which Myoglobin and Hemoglobin escape their
cellular environments and are thus separated from cellular reductive/protective systems, the …

Under normal physiology, human red blood cells (RBCs) demonstrate a circulating lifespan
of∼ 100–120 days with efficient removal of senescent RBCs taking place via the …

Dehaloperoxidase (DHP) is a respiratory hemoglobin (Hb) that has been shown to catalyze
the conversion of trihalophenols to dihaloquinones in the presence of hydrogen peroxide …

Abstract Significance: Erythrocyte hemoglobin (Hb) and myocyte myoglobin, although
primarily oxygen-carrying proteins, have the capacity to do redox chemistry. Such redox …

Heme proteins perform a large array of biological functions using the same heme cofactor. A
primary method of regulating these diverse functions is the heme-protein cross-link, an …

Myoglobin (Mb), an oxygen-binding heme protein highly expressed in heart and skeletal
muscle, has been shown to undergo oxidative modifications on both an inter-and …