Observations on CO trout hemoglobins by <sup>13</sup>C NMR

Giacometti, Giorgio M.; Giardina, Bruno; Brunori, Maurizio; Giacometti, Giovanni; Rigatti, G.

doi:10.1016/0014-5793(76)80042-7

Cited by 14 publications

(10 citation statements)

References 7 publications

(6 reference statements)

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“…This finding is in accord with the results of recent r3C NMR observations which showed unequivocally that at pH 6.0 the (Y and B chains in Hb Trout IV have different CO affinities [6]. The functional differences between o. and p chains, documented in this paper, could be attributed to local, pH-dependent, structural changes, without necessarily excluding the existence of H'-dependent conformational equilibria between high and low affinity states of Hb Trout IV.…”

Section: Discussionsupporting

confidence: 93%

Trout hemoglobin: Oxygen binding at sub‐zero temperatures

Giardina

Brunori

1976

FEBS Letters

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Section: Discussionsupporting

confidence: 93%

Trout hemoglobin: Oxygen binding at sub‐zero temperatures

Giardina

Brunori

1976

FEBS Letters

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“…The pH 6.1 data were interpreted [27] within a model based on (a) non-cooperative O 2 binding to the T-state and (b) very different affinities of the two types of subunits a and b (see the values of n H = 1 below and above Y~0.5). Assigning the two equilibrium phases at pH 6.1 to the a and b subunits is consistent with optical spectroscopy [41] and high-resolution NMR of 13 CO, which clearly discriminates the tertiary structure of the a and b subunits [42].…”

Section: Extreme Heterotropic Controlsupporting

confidence: 73%

Variations on the theme: allosteric control in hemoglobin

Brunori

2013

The FEBS Journal

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Conformational selection between pre‐existing structural states of an oligomeric protein was the conceptual step behind the formulation of Monod–Wyman–Changeux (MWC) allosteric theory. Variations on the basic theme of allosteric control are briefly illustrated in this paper by reference to some hemoglobins from different species whose functional properties were found to respond to specific physiological requirements. In my opinion the enormous success of the allosteric theory may be attributed not only to its efficiency in accounting for data and its formal mathematical elegance, but also because the selective mechanism conforms to the founding concept of Darwinian evolution.

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“…This difference, however, cannot be directly correlated with the overall ligand affinity in view of the previously reported findings by Caughey and coworkers [7] on the CO stretching of hemoglobins, characterized by different affinities. Moreover, these results are significant in relation to the understanding of the Root effect, especially in connection with the information which has been recently obtained by 13C NMR spectroscopy of 13CO-Hb IV [10]. The pH dependence of the resonance of the ligand bound to the ~ and the chains in Hb trout IV shows unequivocally a structural change involving the immediate environment of the ligand binding site.…”

Section: Discussionmentioning

confidence: 60%