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

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 c...

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Bibliographic Details
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
Description
Summary: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.

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