The oxygen-binding intermediates of human hemoglobin: Evaluation of their contributions to cooperativity using zinc-containing hybrids

被引：36

作者：

Huang, YW ^{[1
]}

Doyle, ML ^{[1
]}

Ackers, GK ^{[1
]}

机构：

[1] WASHINGTON UNIV,SCH MED,DEPT BIOCHEM & MOL BIOPHYS,ST LOUIS,MO 63110

来源：

BIOPHYSICAL JOURNAL | 1996年 / 71卷 / 04期

关键词：

D O I：

10.1016/S0006-3495(96)79408-0

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

Hemoglobin tetramers [Zn/FeO2] containing oxygenated subunits (FeO2), in combination with unligated subunits containing zinc-substituted hemes (Zn), were analyzed to determine their contributions to the cooperativity of oxygen binding at the Fe sites. Energetic consequences of possible perturbation by zinc substitution were evaluated in all combinations of unligated Zn/Fe hybrid tetramers, A general thermodynamic strategy that corrects for the energetic effects of substituting a second metal for Fe showed the perturbations of Zn substitution to be negligible, This permitted cooperativity parameters of the native Fe/FeO2 intermediates to be calculated from data on the corresponding Zn/FeO2 molecules, These parameters, determined explicitly for all eight oxygen-binding intermediates (Fe/FeO2), were found to be identical to those predicted earlier from analyzing the O-2 binding data of normal hemoglobin according to the ''molecular code'' of hemoglobin allostery. The cooperativity parameters determined for this system showed the same distribution pattern found previously for five other oxygen analog systems (Fe/FeCN, Fe/Mn3+, Co/FeCO, Co/FeCN, and Fe/FeCO).

引用

页码：2094 / 2105

页数：12

共 51 条

[1]

Ackers G K, 1970, Adv Protein Chem, V24, P343, DOI 10.1016/S0065-3233(08)60245-4

[2] THE ENERGETICS OF LIGAND-LINKED SUBUNIT ASSEMBLY IN HEMOGLOBIN REQUIRE A 3RD ALLOSTERIC STRUCTURE [J].

ACKERS, GK .

BIOPHYSICAL CHEMISTRY, 1990, 37 (1-3) :371-382

[3] ANALYSIS OF HEMOGLOBIN OXYGENATION FROM COMBINED EQUILIBRIUM AND KINETIC DATA - IS QUATERNARY ENHANCEMENT NECESSARY [J].

ACKERS, GK ;

JOHNSON, ML .

BIOPHYSICAL CHEMISTRY, 1990, 37 (1-3) :265-279

[4] LINKAGE BETWEEN OXYGENATION AND SUBUNIT DISSOCIATION IN HUMAN HEMOGLOBIN [J].

ACKERS, GK ;

HALVORSON, HR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1974, 71 (11) :4312-4316

[5] MOLECULAR CODE FOR COOPERATIVITY IN HEMOGLOBIN [J].

ACKERS, GK ;

DOYLE, ML ;

MYERS, D ;

DAUGHERTY, MA .

SCIENCE, 1992, 255 (5040) :54-63

[6] Oxygen binding by single crystals of hemoglobin: The problem of cooperativity and inequivalence of alpha and beta subunits [J].

Bettati, S ;

Mozzarelli, A ;

Rossi, GL ;

Tsuneshige, A ;

Yonetani, T ;

Eaton, WA ;

Henry, ER .

PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1996, 25 (04) :425-437

[7]

CHU AH, 1981, J BIOL CHEM, V256, P1199

[8] EFFECTS OF PROTONS ON THE OXYGENATION-LINKED SUBUNIT ASSEMBLY IN HUMAN-HEMOGLOBIN [J].

CHU, AH ;

TURNER, BW ;

ACKERS, GK .

BIOCHEMISTRY, 1984, 23 (04) :604-617

[9] IDENTIFICATION OF THE INTERMEDIATE ALLOSTERIC SPECIES IN HUMAN HEMOGLOBIN REVEALS A MOLECULAR CODE FOR COOPERATIVE SWITCHING [J].

DAUGHERTY, MA ;

SHEA, MA ;

JOHNSON, JA ;

LICATA, VJ ;

TURNER, GJ ;

ACKERS, GK .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (04) :1110-1114

[10] BOHR EFFECTS OF THE PARTIALLY-LIGATED (CN-MET) INTERMEDIATES OF HEMOGLOBIN AS PROBED BY QUATERNARY ASSEMBLY [J].

DAUGHERTY, MA ;

SHEA, MA ;

ACKERS, GK .

BIOCHEMISTRY, 1994, 33 (34) :10345-10357

← 1 2 3 4 5 6 →