Hemoglobin, Oxygen Transport and Nitric Oxide
This paper presents electron paramagnetic resonance and oxygen binding studies of -nitrosyl hemoglobin - a novel oxygen carrier having NO (Nitric Oxide) assisted allosteric functions.
# 8022 | 1,345 words | 3 sources | APA | 2001 |
Published on Feb 05, 2003 in Biology (Molecular and Cell) , Chemistry (Biochemistry) , Biology (Biotechnology)
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This paper shows that Nitric Oxide (NO) is a very popular compound to investigate in the scientific community today. It is physiologically ubiquitous as a potent vasodilator, neurotransmitter, and immuno-active agent at low concentrations and it is produced and recycled in the respiratory tract to regulate the airway. This paper discusses in detail the mechanism behind oxygen binding and release by hemoglobin as it relates NO bound to the Hemoglobin. The oxygen affinity dynamics of native Hemoglobin and nitrosylated Hb are compared. The research also reveals that although NO has a much higher affinity than oxygen or carbon monoxide for Hemoglobin, NO behaves differently than these other ligands and is not as toxic to normal Hb oxygen binding as previously assumed.
From the Paper:"Small, unicellular aerobic organisms can obtain oxygen required for metabolism by simple diffusion from the environment. Most multicellular organisms have too great a surface area and many cells not in contact with the environment. They require circulatory systems that transport oxygen from gas-exchange organs to other tissues. In vertebrates, oxygen is bound to molecules of Hemoglobin (Hb) or transport in Red Blood Cells. Mammalian Hemoglobin is a tetramer, consisting of four polypeptide chains; two a and two b. Six ligands are coordinated to the ferrous iron, with the ligands in octahedral geometry around the metal cation (figure 1). In aqueous solution, free heme does not does not reversibly bind oxygen. Instead the Fe(II) is rapidly oxidized to Fe(III) when it gives up an electron to oxygen. The quaternary structure of hemoglobin prevents formal transfer of an electron and allows it to reversibly bind O2. Positively charged amino acid residues stabilize to negatively charged diatomic oxygen without an ionic bond. Hemoglobin unbound to oxygen is called deoxyhemoglobin and has a low affinity for oxygen. Once one oxygen molecule binds to the Fe, the proximal Histadine (figure 1) moves closer to the porphyrin ring because the Fe is now bound to six ligands instead of five. This disrupts the stabilizing ions that interact with Hb. The remaining Heme groups have an increased affinity for Oxygen. In addition to this positive cooperatively of binding, allosteric interactions regulate the binding and release of oxygen by Hb (Horton, 1996)."
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