Kinetics of oxygen and carbon monoxide binding to the hemoglobins of Glycera dibranchiata

Parkhurst, Lawrence J.; Sima, Paul D.; Goss, Dixie J.

doi:10.1021/bi00553a023

Cited by 78 publications

(42 citation statements)

References 14 publications

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“…We have previously (Kandler & Satterlee, 1983) sought to reconcile the more extensive heterogeneity that we have found for the Glycera dibranchiata monomer haemoglobin fraction with earlier attempts by Weber et al (1977), Harrington et al (1978) and Parkhurst et al (1980 that indicated less-extensive heterogeneity. Previous attempts at Glycera dibranchiata isolations utilized the protein in the ferrous form (Weber et al, 1977;Harrington et al, 1978;Parkhurst et al, 1980).…”

Section: Separations With Reduced Proteinmentioning

confidence: 68%

“…For ease in handling the protein, which is autoxidizable during the 5-day period necessary for isolation, we chose to isolate the oxidized (ferric) protein except when reproducing previous results with ferrous-CO forms (see below). In fact, we have already indicated (Kandler & Satterlee, 1983) that this proclivity for autoxidation is likely to have contributed to confusing results in a prior Glycera dibranchiata haemoglobin isolation attempt (Parkhurst et al, 1980). Fig.…”

Section: Chemicalsmentioning

confidence: 94%

“…Previous attempts at Glycera dibranchiata isolations utilized the protein in the ferrous form (Weber et al, 1977;Harrington et al, 1978;Parkhurst et al, 1980). Because the isoelectric points of the monomer proteins differ by 0.4pl unit in the ferric and the ferrous states (Kandler & Satterlee, 1983), the slightest neglect of diligence in keeping the proteins in a reducing environment will cause mixtures of oxidation and ligation states within the monomer haemoglobin fraction.…”

Section: Separations With Reduced Proteinmentioning

confidence: 99%

“…These fundamental structural similarities to vertebrate proteins and the concept of a single Glycera dibranchiata monomer haemoglobin stimulated a large amount of work on spectroscopy Harrington et al, 1973Harrington et al, , 1978Kandler & Satterlee, 1983) and ligand binding (Hoffman & Mangum, 1970;Seamonds, 1971;Seamonds & Forster, 1972;Seamonds et al, 1976;Parkhurst et al, 1980). That work was carried out on isolations of the monomer haemoglobin fraction like that from which the crystals were grown.…”

mentioning

confidence: 99%

“…Low-resolution analytical methods (such as separation by Mr, ion-exchange chromatography where the protein pl values were not considered, with incompletely developed columns, and thick-slab low-voltage isoelectric focusing) (Vinogradov et al, 1970;Seamonds et al, 1971;Weber et al, 1977;Harrington et al, 1978) indicated minimal heterogeneity for the monomer. However, Parkhurst et al (1980) more recently suggested a broader heterogeneity that was functional. Subsequently, we have detailed the isolation of four major haemoglobins from the Glycera monomer haemoglobin milieu (Kandler & Satterlee, 1983).…”

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confidence: 99%

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Evaluation of the extent of heterogeneity in the Glycera dibranchiata monomer haemoglobin fraction by the use of n.m.r. and ion-exchange chromatography

Kandler¹,

Constantinidis²,

Satterlee³

1985

Biochemical Journal

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The coelomic haemoglobin of Glycera dibranchiata is known to be separable into monomeric and higher-Mr fractions. Although exhibiting homogeneity with respect to Mr, the extent of haemoglobin heterogeneity for the monomer fraction has never been adequately assayed. In the present paper we demonstrate that there exists in the monomer haemoglobin fraction reproducibly detectable heterogeneity regardless of the presence or absence of proteinase inhibitors during the isolations. These results show that, considered on the same time scale as previous preparations used for amino acid sequencing, crystallography and kinetics, the monomer haemoglobin fraction is highly heterogeneous. Application of ion-exchange chromatography and ionfiltration methods resulted in the isolation of four resolvable haem protein components from the Glycera monomer haemoglobin fraction. Three of these components were isolated in sufficient quantity to employ proton n.m.r. as a successful analytical tool for discriminating the individual haemoglobins. These results are not surprising. Several previous studies indicated less extensive heterogeneity in the monomer fraction. Moreover, the ability of the Glycera monomer haemoglobin to bind oxygen at even quite low partial pressures has been attributed to functional diversity originating in multiple haemoglobin components. The present work reveals the extent of the haemoglobin heterogeneity. The results show that it is more extensive than previously believed. Examination of this monomer fraction is particularly important, since crystallography indicates that one of the components of the monomer fraction lacks the E-7 (distal) histidine residue. As a consequence, the identification of such extensive heterogeneity is important to many previously published ligand-binding studies.

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Section: Separations With Reduced Proteinmentioning

confidence: 68%

Section: Chemicalsmentioning

confidence: 94%

Section: Separations With Reduced Proteinmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Evaluation of the extent of heterogeneity in the Glycera dibranchiata monomer haemoglobin fraction by the use of n.m.r. and ion-exchange chromatography

Kandler¹,

Constantinidis²,

Satterlee³

1985

Biochemical Journal

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Iron Porphyrin Chemistry

Walker¹,

Simonis²

2005

Encyclopedia of Inorganic Chemistry

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This article reviews most aspects of the chemistry of iron porphyrins, from Fe(0) to Fe(V), including occurrence and roles of natural iron porphyrins (hemes) and their synthetic analogs, structures and electron configurations of iron porphyrins of all oxidation and spin states, π electron configuration of the porphyrin ring, synthesis of metal‐free porphyrins and other related macrocycles, insertion of iron into free‐base porphyrins and related macrocycles, the properties, reactions, uses and biological relevance of iron(0), ‐(I), ‐(II) porphyrins (the latter with S = 0, 1, and 2 spin state possibilities), of iron(II) porphyrin π‐cation radicals, of iron(III) porphyrins (with S = 1/2, 3/2, and 5/2 spin state possibilities), of iron(III) porphyrin and corrole π‐cation radicals, of iron(IV) porphyrins (including five‐ and six‐coordinate ferryl (FeO) 2+ , iron(IV) phenyl, carbene and hydrazine complexes, and the bis‐methoxide complex) and a comparison of iron(IV) porphyrins to iron(III) porphyrin π‐cation radicals, of iron(IV) porphyrin π‐cation radicals, and of the possible existence of iron(V) porphyrins. Included in the Fe(II) part are sections on addition of ligands to four‐coordinate iron(II) porphyrins, including equilibrium binding constants, photodissociation of ligands from PFeL 2 complexes, binding of small molecules (O 2 , CO, NO, HNO) to 5‐coordinate iron(II) porphyrins and design of porphyrin ligands that will mimic the active sites of heme proteins such as myoglobin and hemoglobin, the cytochromes P450 and nitric oxide synthases, and the nitrophorins and guanylyl cyclases. Included in the iron(III) part are sections on both 5‐ and 6‐coordinate high‐spin complexes and their similarities and differences, bridged or through‐space magnetically coupled complexes of high‐spin iron(III) porphyrins with other metal complexes as possible models for cytochrome oxidase and the assimilatory sulfite reductases, coupled oxidation of hemes by hydrogen peroxide or its equivalent, and the relationship of this reactivity to the reactions of heme oxygenase, iron(III) porphyrins as reduction catalysts, and photochemistry of iron(III) porphyrins, possible electron configurations of low‐spin iron(III) porphyrins, the phenomenon and possible electronic consequences of ruffling of the porphinato core in iron(III) porphyrins, the preferred orientation of planar axial ligands bound to low‐spin iron(III) porphyrins, NO complexes of iron(III) porphyrins, reduction potentials, equilibrium constants and rates of axial‐ligand addition and exchange, kinetics of axial‐ligand rotation and porphyrin ring inversion, kinetics of reduction and autoreduction of iron(III) porphyrins, electron self‐exchange between low‐spin iron(III) and iron(II) porphyrins, synthetic ferriheme proteins, and synthesis of five‐coordinate low‐spin iron(III) porphyrins having σ‐alkyl or σ‐aryl groups as axial ligands. The iron(IV) and iron(IV) cation radical sections discuss the high‐valent states of cytochromes P450 and related enzymes.

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