Metal ion coordination in 'R' and 'T' state hybrid hemoglobins as revealed by optical, EPR and sulphhydryl reactivity studies
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TLDR
In this paper, the sulphhydryl environment in various mixed-metal hybrid hemoglobins, viz. α2(Cu)-β2(FeCO), α2-FeCO)-β 2(Cu), α 2-Cu-β2-Ni, α 2(Ni)- β2-Cu, β 2-Ni-β 2 (β2)-β 4-PDS, was studied by reacting them with the 4,4′-dithiodipyridine (4PDS) reagent.Abstract:
The sulphhydryl environment in various mixed-metal hybrid hemoglobins, viz. α2(Cu)-β2(FeCO), α2(FeCO)-β2(Cu), α2(Cu)-β2(Ni), α2(Ni)-β2(Cu), was studied by reacting them with the sulphhydryl reagent, 4,4′-dithiodipyridine (4-PDS). The reactivity was compared with that of HbCO, NiHb and CuHb. It is found that there exists a correlation between conformational change and metal ion environment, not only at the extreme R and T states but also the intermediate conformations. EPR examinations of these hybrids show that both in R state-[Cu(II)-Fe(II)] and T state-[Cu(II)-Ni(II)] hybrids at neutral pH and in the absence of IHP, CuPPIX, irrespective of the subunit in which it is present, has a mixed-metal ion environment: Species 1, a five-coordinated Cu2+ complex with strong proximal histidine bond and species 2, a four-coordinated complex without any covalent linkage with Ne F8-histidine.read more
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Studies on nitrosyl hemes in Ni(II)-Fe(II) hybrid hemoglobins.
TL;DR: The bond between N(epsilon) and Fe is fundamental to the structure-function relation in Hb, as the motion of this nitrogen triggers the vast transformation, which occurs in the whole molecule on attachment of NO.
References
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Koichiro Ishimori,Isao Morishima +1 more
TL;DR: The proton NMR spectra of the intersubunit hydrogen-bonded protons showed that the quaternary structures of the two complementary hybrids both remain in the "T-like state" at low pH, suggesting that the T to R structural conversion is induced by ligation of the third ligand molecule.
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TL;DR: The circular dichroism of the porphyrin transitions suggests that the packing of the amino acid side chains around the p Morphyrin is different than that in the native metmyoglobin.
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Proton nuclear magnetic resonance investigation of cross-linked asymmetrically modified hemoglobins: influence of the salt bridges on tertiary and quaternary structures of hemoglobin
Shigetoshi Miura,Chien Ho +1 more
TL;DR: The experimental results indicate that the effects on the hyperfine-shifted proximal histidyl N delta H exchangeable proton resonances at pH 6.0 of removing Arg(alpha 141) or Arg( alpha 141)-Tyr(alpha 140) from one of the two alpha subunits are limited to within the alpha subunit from which the carboxyl-terminal amino acids are specifically removed.
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Metal-ion coordination in copper and nickel reconstituted hemoglobins
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The structure of partially oxygenated hemoglobin. A highly reactive intermediate toward a sulfhydryl titrant.
TL;DR: It was concluded that the ligand-linked structural changes in hemoglobin take place through several steps, and the existence of another molecular species with an intermediate reactivity between those of oxy and deoxy forms was suggested.