Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin

Paolo Ascenzi; Roberto Santucci; Alessandro Desideri; Gino Amiconi

doi:10.1016/0162-0134(88)85001-3

Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin

Paolo Ascenzi, Roberto Santucci, Alessandro Desideri, Gino Amiconi

Istituto Nazionale per le Malattie Infettive Lazzaro Spallanzani

Research output: Contribution to journal › Article › peer-review

Abstract

The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopie (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.

Original language	English
Pages (from-to)	225-232
Number of pages	8
Journal	Journal of Inorganic Biochemistry
Volume	32
Issue number	4
DOIs	https://doi.org/10.1016/0162-0134(88)85001-3
Publication status	Published - 1988

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

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10.1016/0162-0134(88)85001-3

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title = "Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin",

abstract = "The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopie (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.",

author = "Paolo Ascenzi and Roberto Santucci and Alessandro Desideri and Gino Amiconi",

year = "1988",

doi = "10.1016/0162-0134(88)85001-3",

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pages = "225--232",

journal = "Journal of Inorganic Biochemistry",

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T1 - Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin

AU - Ascenzi, Paolo

AU - Santucci, Roberto

AU - Desideri, Alessandro

AU - Amiconi, Gino

PY - 1988

Y1 - 1988

N2 - The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopie (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.

AB - The effect of inositol hexakisphosphate, 2,3-diphosphoglycerate, dextran sulphate, and heparin on the spectroscopie (absorbance, circular dichroism, EPR) properties of the nitric oxide derivative of ferrous dromedary (Camelus dromedarius) hemoglobin was investigated. The results obtained show that: (i) all polyanions bind to the protein at the same sites, but with different affinities; (ii) polyanions affect the protein conformation of the ferrous nitrosyl derivative in a different way with respect to aquo-ferric and ferrous oxy dromedary hemoglobin; and (iii) the data obtained provide further independent evidence for the existence in dromedary hemoglobin of two functionally distinct polyanion binding sites that affect the conformational equilibrium of the protein in opposite ways.

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Effect of polyanions on the spectroscopic properties of the nitric oxide derivative of ferrous dromedary (camelus dromedarius) hemoglobin

Abstract

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