Hemoglobin (Hb) plays its vital role through structural and functional properties
evolutionarily optimized to work within red blood cells, ie, the tetrameric assembly, well …

The search for a clinically affordable substitute of human blood for transfusion is still an
unmet need of modern society. More than 50 years of research on acellular hemoglobin …

The development of hemoglobin (Hb)-based oxygen carriers (HBOCs) has been hampered
because of safety concerns in humans. Chemical and/or genetic modifications of the Hb …

Hemoglobin functions as a tetrameric oxygen transport protein, with each subunit containing
a heme cofactor. Its denaturation, either in vivo or in vitro, involves autoxidation to …

Redox active cysteine residues including βCys93 are part of hemoglobin's “oxidation
hotspot”. Irreversible oxidation of βCys93 ultimately leads to the collapse of the hemoglobin …

The extinct Steller's sea cow (Hydrodamalis gigas;† 1768) was a whale-sized marine
mammal that manifested profound morphological specializations to exploit the harsh coastal …

Thermosynechococcus elongatus-BP1 belongs to the class of photoautotrophic
cyanobacterial organisms. The presence of chlorophyll a, carotenoids, and phycocyanobilin …

The highly toxic oxidative transformation of hemoglobin (Hb) to the ferryl state (HbFe4+) is
known to occur in both in vitro and in vivo settings. We recently constructed oxidatively …

Cell free hemoglobin (Hb), becomes oxidized in the circulation during hemolytic episodes in
sickle cell disease (SCD) or thalassemia and may potentially cause major complications that …

After reacting with hydrogen peroxide (H 2 O 2), sickle-cell hemoglobin (HbS, βE6V)
remains longer in a highly oxidizing ferryl form (HbFe 4+= O) and induces irreversible …