Reversible Dioxygen Binding

Gersonde, Klaus

doi:10.1007/978-3-642-69467-7_9

Cited by 7 publications

(4 citation statements)

References 61 publications

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“…However, the individual bond lengths (then the corresponding bond strength) of Fe-O(0) and Fe-N(F8His) are known to be codependent, as well as with the 0-0 bond (Gersonde 1983). For instance, a decrease or increase of the iron-imidazole bond distance leads to the increase or decrease, respectively, of the Fe-O(0) bond length.…”

Section: Effect Of Glutaraldehyde On Nitrosyl Hemoglobin Epr Spectramentioning

confidence: 99%

“…For instance, a decrease or increase of the iron-imidazole bond distance leads to the increase or decrease, respectively, of the Fe-O(0) bond length. On the other hand, an increase or a decrease of the 0-0 bond is correlated to a decrease or increase, respectively, of the Fe-O(0) bond length (Gersonde 1983;Thompson et al 1987).…”

Section: Effect Of Glutaraldehyde On Nitrosyl Hemoglobin Epr Spectramentioning

confidence: 99%

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Glutaraldehyde effect on hemoglobin: evidence for an ion environment modification based on electron paramagnetic resonance and Mossbauer spectroscopies

Chevalier¹,

Guillochon²,

Nedjar³

et al. 1990

Biochem. Cell Biol.

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Glutaraldehyde is a widely used reagent for hemoglobin cross-linking in blood substitutes research. However, hemoglobin polymerization by glutaraldehyde involves modifications of its functional properties, such as oxygen affinity, redox potentials, and autoxidation kinetics. The aim of this article is to investigate, by electron paramagnetic resonance and Mossbauer spectroscopies, the changes that occur in the iron environment after glutaraldehyde cross-linking. Spectrometric studies were performed with native hemoglobin and hemoglobin cross-linked as soluble and insoluble polymers. Spectrometry data comparison with glutaraldehyde-modified hemoglobin functional properties allows to interpret from a structural point of view that glutaraldehyde action occurs as a decrease of the O--N(F8His) distance, an increase of the Fe--N(F8His) bond length, and the decrease of the distal-side steric hindrance.

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Section: Effect Of Glutaraldehyde On Nitrosyl Hemoglobin Epr Spectramentioning

confidence: 99%

Section: Effect Of Glutaraldehyde On Nitrosyl Hemoglobin Epr Spectramentioning

confidence: 99%

Glutaraldehyde effect on hemoglobin: evidence for an ion environment modification based on electron paramagnetic resonance and Mossbauer spectroscopies

Chevalier¹,

Guillochon²,

Nedjar³

et al. 1990

Biochem. Cell Biol.

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“…The hemoglobin from insect larvae of Chironomus thummi thummi (CTT III) is an interesting model system for understanding the mechanisms of protein control of heme reactivity (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12). It is a monomeric allosteric hemoglobin exhibiting a Bohr effect, which can be correlated with a conformational transition (t-*r) controlled by a single proton, as shown by ESR (2)(3)(4)(5)(6) and NMR (3,(7)(8)(9)(10)(11)(12) studies.…”

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confidence: 99%

“…It is a monomeric allosteric hemoglobin exhibiting a Bohr effect, which can be correlated with a conformational transition (t-*r) controlled by a single proton, as shown by ESR (2)(3)(4)(5)(6) and NMR (3,(7)(8)(9)(10)(11)(12) studies. This allosteric conformational transition and the ligand affinity are modulated by the trans effect of the proximal histidine, the direct interaction of the exogenous ligand with its microenvironment, the protein-'porphyrin interactions, and the electronic structure of the heme iron (1,5). It has been demonstrated (3,7,13,14) that the amplitude of the Bohr-effect curve, a measure of the interaction energy between the Bohr-proton binding site and the ligand binding site, depends on the nature of the exogenous ligand.…”

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confidence: 99%

Iron-carbon bond lengths in carbonmonoxy and cyanomet complexes of the monomeric hemoglobin III from Chironomus thummi thummi: a critical comparison between resonance Raman and x-ray diffraction studies.

Yu¹,

Benko²,

Kerr³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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the porphyrin system and the hindering distal amino acid side group to change their positions so that the whole ligandheme-protein system again reaches an energy minimum. In contrast to a ligand-heme model system, the structure of liganded hemoglobin is extremely sensitive to temperature and electrostatic interaction (variations in salt concentration and pH). Bond length and binding geometry may therefore be sensitive indicators of the actual state of the ligandheme-protein interactions in hemoglobins. Since the numerous conformations of this system may be removed in a crystal, one needs more information about these subtle interactions in solution and under physiological conditions. At present, there is evidence that the fine-structure of CTT III in solution is not the same as it is in crystals. By proton NMR in solution (8,19), CTT III has been shown to exist in two forms, which differ in heme orientation, related by an t180°r otation about the a,-y-meso axis at least in the metHbCN

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Der anorganische Naturstoff O2: Aufnahme, Transport und Speicherung

Kaim

Schwederski

1995

Teubner Studienbücher Chemie

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Reversible Dioxygen Binding

Cited by 7 publications

References 61 publications

Glutaraldehyde effect on hemoglobin: evidence for an ion environment modification based on electron paramagnetic resonance and Mossbauer spectroscopies

Glutaraldehyde effect on hemoglobin: evidence for an ion environment modification based on electron paramagnetic resonance and Mossbauer spectroscopies

Iron-carbon bond lengths in carbonmonoxy and cyanomet complexes of the monomeric hemoglobin III from Chironomus thummi thummi: a critical comparison between resonance Raman and x-ray diffraction studies.

Der anorganische Naturstoff O2: Aufnahme, Transport und Speicherung

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