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Titolo:
Spectroscopic contributions to the understanding of hemoglobin function: Implications for structural biology
Autore:
Shulman, RG;
Indirizzi:
Yale Univ, Dept Mol Biophys & Biochem, New Haven, CT 06510 USA Yale Univ New Haven CT USA 06510 ophys & Biochem, New Haven, CT 06510 USA
Titolo Testata:
IUBMB LIFE
fascicolo: 6, volume: 51, anno: 2001,
pagine: 351 - 357
SICI:
1521-6543(200106)51:6<351:SCTTUO>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
COOPERATIVE OXYGEN-BINDING; ABSORPTION FINE-STRUCTURE; X-RAY-DIFFRACTION; T-STATE; ALLOSTERIC MODEL; KINETICS; STEREOCHEMISTRY; DISTANCES; CRYSTALS; SPECTRA;
Keywords:
hemoglobin; Monod-Wyman-Chageuk; NMR; X-ray structure;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Shulman, RG Yale Univ, Dept Mol Biophys & Biochem, POB 6666, New Haven, CT06510 USA Yale Univ POB 6666 New Haven CT USA 06510 Haven, CT 06510 USA
Citazione:
R.G. Shulman, "Spectroscopic contributions to the understanding of hemoglobin function: Implications for structural biology", IUBMB LIFE, 51(6), 2001, pp. 351-357

Abstract

Structural biology is based on the assumption that structural determinations will explain macromolecular function. To examine the basis of these proposals, the structure/function connections in hemoglobin have been examined. Presently the Monod, Wyman, Changeux (MWC) model of hemoglobin function has great validity. In this model, ligand-binding affinities are linked to quaternary structure, and it has been shown that the model describes the function accurately to a high first approximation. To see how this understanding developed, we review two sets of experimental studies in 1970-71 that supported the applicability of MWC to hemoglobin oxygen binding. One set of data from NMR and ligan binding kinetics supported the quaternary-linked nature of binding required by the MWC model. The other approach, by Perutz, proposed a structural basis for MWC, by suggesting that in one quaternary structure the binding of oxygen broke a salt bridge that caused a lowered quaternary-linked affinity. However, experiments since that time, mostly by X-ray crystallography of deoxygenated hemoglobin, have failed to show salt bridges breaking upon ligation, whereas affinities have remained low. This pattern of results shows that the small energies responsible for ligand-bindingaffinities and reaction rates have not been identified by discrete structural features. Rather, thermodynamic and kinetic data from a variety of spectroscopic studies have played the central role in establishing the MWC model for hemoglobin.

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Documento generato il 23/09/20 alle ore 13:02:37