Literature DB >> 708796

[The hemoglobin molecule from a cybernetic and thermodynamic point of view (author's transl)].

K Trincher.   

Abstract

The biological macromolecule hemoglobin (Hb) represents a reversibly functioning molecular machine. The Hb molecule is engaged in inner or structural work, which is cyclic in nature and is regulated through an exchange with the external milieu, of warmth and matter. The endothermic process of deoxygenation requires an external milieu that gives off warmth and that absorbs oxygen; the exothermic process of oxygenation, on the other hand, requires an external milieu that absorbs warmth and gives up oxygen. The Hb molecule exists in two extreme states: in a signal state for oxygenation and in a target state for deoxygenation. The transition from the signal to the target state occurs via the information process that is coupled to the structural work of the Hb molecule, whereby the absorbed warmth is converted via the structural work, without loss of energy, into the structural energy of the Hb molecule.

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Year:  1978        PMID: 708796     DOI: 10.1007/bf00337142

Source DB:  PubMed          Journal:  Biol Cybern        ISSN: 0340-1200            Impact factor:   2.086


  4 in total

1.  The determination of the individual equilibrium constants of the four intermediate reactions between oxygen and sheep haemoglobin.

Authors:  F J ROUGHTON; A B OTIS; R L LYSTER
Journal:  Proc R Soc Lond B Biol Sci       Date:  1955-08-16

2.  The thermochemistry of the oxygen-haemoglobin reaction: Comparison of the heat as measured directly on purified haemoglobin with that calculated indirectly by the Van't Hoff Isochore.

Authors:  F J Roughton; G S Adair; J Barcroft; G Goldschmidt; W Herkel; R M Hill; A B Keys; G B Ray
Journal:  Biochem J       Date:  1936-11       Impact factor: 3.857

3.  [Thermodynamics of conformational changes in hemoglobin].

Authors:  K S Trintscher
Journal:  Z Naturforsch B       Date:  1972-05       Impact factor: 1.047

4.  The Croonian Lecture, 1968. The haemoglobin molecule.

Authors:  M F Perutz
Journal:  Proc R Soc Lond B Biol Sci       Date:  1969-05-20
  4 in total

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