Properties of the α and β Chains of Hemoglobin Prepared from Their Mercuribenzoate Derivatives by Treatment with 1-Dodecanethiol

Renzo, E.C. De; Ioppolo, Carmela; Amiconi, Gino; Antonini, Eraldo; Wyman, Jeffries

doi:10.1016/s0021-9258(18)99449-4

Cited by 83 publications

(6 citation statements)

References 13 publications

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“…Moreover, the present experiments show that reconstitution of functionally normal hemoglobin from globin and heme can take place in steps, with first addition of heme to the «-chain globin and then binding of heme to the ß chains. Taken together with recent studies on the reconstitution of hemoglobin from isolated «h and /3b chains (Bucci and Fronticelli, 1965;Antonini et al, 1966;De Renzo et al, 1967) these results confirm the conclusion that no matter how the final stoichiometric mixture is achieved, the hemoglobin molecule, with all its attributes, is spontaneously reassembled by simply mixing its components (Antonini, 1967). The results reported here for «b/3 are at variance with those obtained by Banerjee and Cassoly (1967) which indicated that the «-heme /3-chain compound could not be readily converted into hemoglobin, since it maintained the abnormal functional properties even after saturation with heme.…”

Section: Discussionsupporting

confidence: 79%

Functional properties of a hemoglobin carrying heme only on α-chains

Winterhalter¹,

Amiconi²,

Antonini³

1968

Biochemistry

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Section: Discussionsupporting

confidence: 79%

Functional properties of a hemoglobin carrying heme only on α-chains

Winterhalter¹,

Amiconi²,

Antonini³

1968

Biochemistry

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“…A value of -18.1 ± 0.3 kcal/mol was obtained for the reaction of horse myoglobin with CO(g) (Rudolph et al. 1972). De Renzo et al (1967 have reported a value of -13.5 kcal/ mol of O2 as determined by the temperature dependence of the equilibrium constant for reaction of 02(g) with either separate a-or /3-chain solutions.…”

Section: Resultsmentioning

confidence: 97%

Heats of carbon monoxide binding by hemoglobin M Iwate

Ht¹,

Sj²,

Bg³

et al. 1975

Biochemistry

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The heat of reaction of CO gas with the alpha2Mmetbeta2 and alpha2Mbeta2 species of the alpha-chain mutant hemoglobin M Iwate has been studied in buffers with different heats of ionization of 25degrees and in the absence of organic phosphates. For the alpha2Mmetbeta2deoxy species we find a small Bohr effect (0.12 mol of H+/mol of CO) which is in correspondence with that found in equilibrium studies. The heat of reaction, when corrected for proton reaction with buffer, is -18.4 +/- 0.3 kcal/mol of CO at pH 7.4 At pH 9 the same value is observed within experimental error. This value compares closely with heats of reaction of CO with myoglobin and with van't Hoff determinations of the heat of oxygen binding to isolated hemoglobin alpha and beta chains after correction for the heat of replacement of O2 by CO. Furthermore, an analysis of the differential heat of ligand binding as a function of the extent of reaction indicated that, within experimental error, the heat of reaction with the first beta-chain heme in alpha2Mmetbeta2deoxy is the same as the second. Since the quaternary Tleads to R transition is blocked in this mutant hemoglobin, we compared it with Hb A to estimate the enthalpic component of the allosteric T leads to R transition in Hb A. The heats of reaction with CO(g) and Hb A are -15.7 +/- 0.5 and -20.9 +/- 0.5 kcal/mol at pH 7.4 and 9.0, respectively. In going from the T to the R state we find an enthalpy of transition of 9 +/- 2.5 kcal at pH 7.4 and -12 +/- 2.5 kcal at pH 9.0. From published free energies of transsition we conclude the T leads to R transition is enthalpically controlled at p/ 7.4 but entropically controlled at pH 9.0 A near normal Bohr effect is estimated from heats of reaction of CO with alpha2Mdeoxybeta2deoxy in various buffers. A large than normal heat of reaction (-21.6 +/- 0.5 kcal/mol of CO) is attributed to the abnormal alpha chains in Hb M Iwate.

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“…a and ß chains of human hemoglobin were prepared with regenerated sulfhydryl groups (designated a$H and (3sh) by the method of Geraci et al (1969) with minor modifications. Electrophoretic patterns of ferrous asn and /3sh preparations and of normal ferrihemoglobin, obtained by polyacrylamide gel electrophoresis, exhibited the appropriate relative mobilities (De Renzo et al, 1967). The $ and (3sh chains were converted to the ferric form with ferricyanide and the latter reagent was removed by passage over a Bio-Gel P-2 column.…”

Section: Methodsmentioning

confidence: 99%

Association of methanol and ethanol with heme proteins

As¹,

Bw²,

Me³

1976

Biochemistry

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The behavior of ferrihemoglobin and ferrimyoglobin in widely varying concentrations of the lowest four alcohols has been studied by optical and electron paramagnetic resonance absorption spectroscopy. Methanol and ethanol, at concentrations too low to cause general conformational destabilization of the protein, produce both optical and electron paramagnetic resonance absorption spectral changes in ferrihemoglobin. These changes arise from equilibrium associations, characterized by dissociation constants at 25 degrees C of about 40 and 200 mM, respectively, for the methanol-ferrihemoglobin and ethanol-ferrihemoglobin complexes so formed. Other optical spectral changes appear when the methanol concentration exceeds 3.5 M and the ethanol, 1.0 M. At concentrations lower than 0.5 M, 1- and 2-propanol produce spectral changes of this second kind. At room temperature no optical evidence has been found that the propanols associate with ferrihemoglobin in the manner of methanol and ethanol. Methanol and ethanol at low concentration have specific effects, characterized by electron paramagnetic resonance spectral differences, upon ferric alphaSH chains. All four alcohols, over a wide range of concentrations, reduce the symmetry of electron paramagnetic resonance spectra from frozen solutions of ferrihemoglobin; even at the high end of this concentration range, none of the alcohols reduces the symmetry of electron paramagnetic resonance spectra from frozen ferrimyoglobin. Ferrimyoglobin and catalase association with methanol is measurable optically; the binding is about five and sixty times weaker, respectively, for these two proteins as compared with ferrihemoglobin.

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Properties of the α and β Chains of Hemoglobin Prepared from Their Mercuribenzoate Derivatives by Treatment with 1-Dodecanethiol

Cited by 83 publications

References 13 publications

Functional properties of a hemoglobin carrying heme only on α-chains

Functional properties of a hemoglobin carrying heme only on α-chains

Heats of carbon monoxide binding by hemoglobin M Iwate

Association of methanol and ethanol with heme proteins

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