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Volume 271, Number 47, Issue of November 22, 1996 pp. 29859-29864
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Proton-linked Subunit Kinetic Heterogeneity for Carbon Monoxide Binding to Hemoglobin from Chelidonichthys kumu

(Received for publication, May 24, 1996, and in revised form, August 5, 1996)

Massimo Coletta , Paolo Ascenzi ^¶ , Rossana D'Avino and Guido di Prisco

From the  Department of Molecular, Cellular and Animal Biology, University of Camerino, Via Filippo Camerini 2, 62032 Camerino (MC), the ^¶ Department of Biology, Third University of Rome, Via Ostiense 173, 00154 Rome, and the  Consiglio Nazionale delle Ricerche, Institute of Protein Biochemistry and Enzymology, Via G. Marconi 10, 80125 Naples, Italy

The pH dependence of CO binding kinetics to Chelidonichthys kumu hemoglobin (Hb) and human adult Hb has been investigated between pH 2.0 and 9.0 at 20 °C. For both Hbs, CO binding kinetics is characterized by two proton-linked transitions, with different pK_a values for - and -chains in C. kumu Hb, leading to a relevant functional kinetic heterogeneity at most pH values. On the other hand, in human adult Hb the CO binding does not display a functional heterogeneity. Lowering the pH from 9 to 6 brings about a decrease of the CO binding rate constants, to a different extent for human adult Hb and the two chains of C. kumu Hb. Further lowering the pH from 6 to 2 induces an enhancement of CO binding rate constants, probably related to the protonation of proximal His^F8 N atom and the cleavage (or severe weakening) of the His^F8-Fe bond. The presence of physiological concentrations of ATP (3 mM) affects the pH dependence of CO binding kinetics to C. kumu. Moreover, the effect of temperature (between 8 °C and 38 °C) on CO binding kinetics has been investigated in the absence of ATP at different pH values. These results allow to interpret the functional kinetic heterogeneity of C. kumu Hb on the basis of different regulatory aspects in the - and -subunits, as suggested by structural considerations.

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