Interaction of haemoglobin with ions binding of inositol hexaphosphate to human haemoglobin a

Jänig, G.-R.; Ruckpaul, K; Jung, F.; Jung, Woo‐Sik; Grill, H. J.

doi:10.1016/0014-5793(71)80141-2

Cited by 34 publications

(12 citation statements)

References 20 publications

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“…Inspection of the cavity clearly shows that steric constraints would be too high to accommodate a second effector, in good agreement with reported 1:1 binding stoichiometries for R-state HbA [16,18,19].…”

Section: Resultssupporting

confidence: 86%

“…Due to the high computational cost of our study, we did not attempt to dock a second effector to our R-models, thus it is entirely possible that a second site may be present, but not in the central cavity. Inspection of the cavity clearly shows that steric constraints would be too high to accommodate a second effector, in good agreement with reported 1:1 binding stoichiometries for R-state HbA [16,18,19].…”

Section: Resultssupporting

confidence: 86%

“…In this view, effectors lower the oxygen affinity by stabilizing the Tstate salt bridges between the b-subunits as they bind the larger T-state central cavity. Yet, a considerable body of experimental evidence had long shown that heterotropic effectors did interact not only with T, but also with R-state HbA [16][17][18][19][20]. DPG was reported to specifically bind both R-and T-state HbA, albeit the T-state $50% more strongly [16] while IHP was observed to bind the R-state even more strongly than the T-state [18].…”

Section: Introductionmentioning

confidence: 99%

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R‐state hemoglobin bound to heterotropic effectors: models of the DPG, IHP and RSR13 binding sites

Laberge¹,

Kovesi²,

Yonetani³

et al. 2004

FEBS Letters

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We performed a docking study followed by a 500-ps molecular dynamics simulation of R-state human adult hemoglobin (HbA) complexed to different heterotropic effectors [2,3-diphosphoglycerate (DPG), inositol hexaphosphate (IHP), and 2-[4-[(3,5-dichlorophenylcarbamoyl)-]methyl]-phenoxy]-2-methylpropionic acid (RSR13)) to propose a molecular basis for recently reported interactions of effectors with oxygenated hemoglobin. The simulations were carried out with counterions and explicit solvation. As reported for T-state HbA, the effector binding sites are also located in the central cavity of the R-state and differ depending on effector anionic character. DPG and IHP bind between the a-subunits and the RSR13 site spans the a 1 -, a 2 -and b 2 -subunits. The generated models provide the first report of the molecular details of R-state HbA bound to heterotropic effectors.

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Section: Resultssupporting

confidence: 86%

Section: Resultssupporting

confidence: 86%

Section: Introductionmentioning

confidence: 99%

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R‐state hemoglobin bound to heterotropic effectors: models of the DPG, IHP and RSR13 binding sites

Laberge¹,

Kovesi²,

Yonetani³

et al. 2004

FEBS Letters

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“…Information on IHP binding is more consistent. IHP binds to HbCO A and methemoglobin A in a ratio of one per tetramer (Janig et al, 1971; Gray and Gibson, 1971;Tyuma et al, 1971). Perutz et al (1972)2 suggested that the IHP-methemoglobin A binding site is similar to the site of DPG-deoxyHb A binding proposed by Bunn and Briehl (1970) and recently by Arnone (1972).…”

Section: Discussionmentioning

confidence: 90%

Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobin

Lindstrom¹,

Ho²

1973

Biochemistry

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“…P2 glycerate binds weakly to oxyhemoglobin (18,19), but the binding is increased as the pH falls below 7 (19). IP6 binds to both oxyand deoxyhemoglobin (10,20,21). The high concentration of organic phosphate used in this study insures that the par-tially liganded intermediates bind phosphate, and are presumably stabilized in low affinity forms.…”

Section: Discussionmentioning

confidence: 91%

Functional Nonequivalence of α and β Hemes in Human Adult Hemoglobin

Lindstrom

1972

Proc. Natl. Acad. Sci. U.S.A.

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Nuclear magnetic resonance studies of the contact-shifted spectra of heme protons in deoxyhemoglobin A from human adults show conclusively that oxygen binds to the a hemes in preference to the fi hemes. (9). Perutz further describes how 2,3-diphosphoglycerate(P2 glycerate) and hydrogen ion inhibit-the structural transition from the deoxy to the oxy quaternary structure (9). Based on indirect kinetic and spectroscopic evidence, Gray and Gibson (10) have proposed that CO combines first with the fi chains before the a chains. As yet, there is no direct experimental evidence showing that oxygen binds to one type of heme in Rb A in preference to another. This is a preliminary report on the preferential binding of oxygen to the a-chain hemes in the presence of P2 glycerate or inositol hexaphosphate(1P6), as monitored by selective decrease of the contact-shifted resonances of the a chains. MATERIALS AND METHODSHbCO A was prepared (11)

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Interaction of haemoglobin with ions binding of inositol hexaphosphate to human haemoglobin a

Cited by 34 publications

References 20 publications

R‐state hemoglobin bound to heterotropic effectors: models of the DPG, IHP and RSR13 binding sites

R‐state hemoglobin bound to heterotropic effectors: models of the DPG, IHP and RSR13 binding sites

Effects of anions and ligands on the tertiary structure around ligand binding site in human adult hemoglobin

Functional Nonequivalence of α and β Hemes in Human Adult Hemoglobin

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