Literature DB >> 4514980

Interpretation of the binding of carbon monoxide to hemoglobin under photodissociating conditions.

A Szabo, M Karplus.   

Abstract

An interpretation is given of recent experiments by Brunori et al. on the binding of carbon monoxide by hemoglobin under photodissociating conditions. It is shown that their results follow directly from scalable models for hemoglobin in which the protein-modulated interactions are separable from the ligand binding.

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Year:  1973        PMID: 4514980      PMCID: PMC433332          DOI: 10.1073/pnas.70.3.673

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  6 in total

1.  ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.

Authors:  J MONOD; J WYMAN; J P CHANGEUX
Journal:  J Mol Biol       Date:  1965-05       Impact factor: 5.469

2.  Thermochemistry of the oxygen-haemoglobin reaction: Direct measurements of the heat of reaction under various conditions.

Authors:  F J Roughton
Journal:  Biochem J       Date:  1935-11       Impact factor: 3.857

3.  The Oxygen Equilibrium of Hemoglobin and Its Structural Interpretation.

Authors:  L Pauling
Journal:  Proc Natl Acad Sci U S A       Date:  1935-04       Impact factor: 11.205

4.  Carbon monoxide binding by hemoglobin and myoglobin under photodissociating conditions.

Authors:  M Brunori; J Bonaventura; C Bonaventura; E Antonini; J Wyman
Journal:  Proc Natl Acad Sci U S A       Date:  1972-04       Impact factor: 11.205

5.  A mathematical model for structure-function relationships in hemoglobin.

Authors:  A Szabo; M Karplus
Journal:  Biochem Biophys Res Commun       Date:  1972-01-31       Impact factor: 3.575

6.  Mechanism of cooperative oxygen binding to hemoglobin (spin-labeled triphosphate-concerted transition model-hemoglobin chesapeake).

Authors:  R T Ogata; H M McConnell
Journal:  Proc Natl Acad Sci U S A       Date:  1972-02       Impact factor: 11.205

  6 in total
  3 in total

1.  Simplifications of the derivations and forms of steady-state equations for non-equilibrium random substrate-modifier and allosteric enzyme mechanisms.

Authors:  E P Whitehead
Journal:  Biochem J       Date:  1976-12-01       Impact factor: 3.857

2.  The kinetics of conformational changes in hemoglobin, studied by laser photolysis.

Authors:  B Alpert; R Banerjee; L Lindqvist
Journal:  Proc Natl Acad Sci U S A       Date:  1974-02       Impact factor: 11.205

3.  Heme proteins: quantum yield determined by the pulse method.

Authors:  M Brunori; G M Giacometti; E Antonini; J Wyman
Journal:  Proc Natl Acad Sci U S A       Date:  1973-11       Impact factor: 11.205

  3 in total

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