Spectroscopic properties of the nitric oxide derivative of ferrous man, horse, and ruminant hemoglobins: a comparative study

• Main Authors: Ascenzi, P, Petruzzelli, R, Bolognesi, M, Giardina, B., COLETTA, MASSIMILIANO, DESIDERI, ALESSANDRO, POLIZIO, FRANCESCA, CONDO', SAVERIO GIOVANNI
• Other Authors: Coletta, M, Desideri, A, Polizio, F, Condo', Sg, Giardina, B
• Format: Article in Journal/Newspaper
• Language: English
• Published: 1992
• Subjects: Morpholine; Animal; Models; Molecular; Human; Hydrogen-Ion Concentration; Horse; Ruminant; Reindeer; Nitric Oxide; Cattle; Hemoglobin; Alkanesulfonate; Electron Spin Resonance Spectroscopy; Buffaloe; Spectrophotometry; Alkanesulfonic Acid; Allosteric Regulation; Deer; Protein Conformation; Settore BIO/10 - BIOCHIMICA; musk ox
• Online Access: http://hdl.handle.net/2108/54783

The spectroscopic (EPR and absorbance) properties of the nitric oxide derivative of ferrous man, horse, buffalo, deer, mouflon, musk ox, ox, and reindeer hemoglobin (HbNO) have been investigated in the absence of any allosteric effector at pH 6.5 (in 0.1 M 2-[N-morpholino]ethanesulphonic acid/NaOH chloride-free buffer system), as well as at 100 K and/or 20 degrees C. Man and horse HbNO show spectroscopic properties that are generally taken as typical of the high affinity state of ferrous tetrameric Hb's; on the other hand, the spectroscopic properties of ruminant (i.e., buffalo, deer, mouflon, musk ox, ox, and reindeer) HbNO are characteristic of the low affinity conformation. These results are in keeping with the functional properties of the mammalian Hb's considered and have been related to the peculiar low oxygen affinity of ruminant Hb's.