Primary structure of aplysia myoglobin: Sequence of a 63‐residue fragment

Tentori, L; Vivaldi, G; Carta, Salvatore; Marinucci, M; Massa, A.; Antonini, Eraldo; Brunori, Maurizio

doi:10.1016/0014-5793(71)80015-7

Cited by 19 publications

(7 citation statements)

References 10 publications

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“…differentiate it from the more commonly studied mammalian Mbs. A number of structural and functional studies have indicated that the most relevant substitution at the heme site responsible for the unique properties of this protein is the absence of a distal histidine (Tentori et al, 1971), which is substituted with a residue (probably a lysine) suggested to be partially turned out of the heme pocket toward the solvent (Bolognesi et al, 1985). Oxygen dissociation kinetics are about 7-fold more rapid (Wittenberg et al, 1965) than in horse heart Mb, in agreement with the structural findings.…”

supporting

confidence: 75%

NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements

Pande¹,

Mar²,

Lecomte³

et al. 1986

Biochemistry

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The 1H NMR characteristics of the high-spin metmyoglobin from the mollusc Aplysia limacina have been investigated and compared with those of the myoglobin (Mb) from sperm whale. Aplysia metMb exhibits a normal acid----alkaline transition with pK approximately 7.8. In the acidic form, the heme methyl and meso proton resonances have been assigned by 1H NMR using samples reconstituted with selectively deuterated hemins and in the latter case by 2H NMR as well. On the basis of the methyl peak intensities and shift pattern, heme rotational disorder could be established in Aplysia Mb; approximately 20% of the protein exhibits a reversed heme orientation compared to that found in single crystals. Three meso proton resonances have been detected in the upfield region between -16 and -35 ppm, showing that the chemical shift of such protons can serve as a diagnostic probe for a pentacoordinated active site in hemoproteins, as previously shown to be the case in model compounds. The temperature dependence of the chemical shift of the meso proton signals deviates strongly from the T-1 Curie behavior, reflecting the presence of a thermally accessible Kramers doublet with significant S = 3/2 character. Nuclear Overhauser effect, NOE, measurements on Aplysia metMb have provided the assignment of individual heme alpha-propionate resonances and were used to infer spatial proximity among heme side chains. The hyperfine shift values for assigned resonances, the NOE connectivities, and the NOE magnitudes were combined to reach a qualitative picture of the rotational mobility and the orientation of the vinyl and propionate side chains of Aplysia metMb relative to sperm whale MbH2O.(ABSTRACT TRUNCATED AT 250 WORDS)

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supporting

confidence: 75%

NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements

Pande¹,

Mar²,

Lecomte³

et al. 1986

Biochemistry

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“…Carboxypeptidase A digestion performed on the globin have shown the carboxy-terminal sequence to be -His Ala-Leu. Thus, as in all other myoglobins and hemoglobins below the vertebrate evolutionary level [7,8,311, this hemoglobin also lacks tyrosine (H22). As preliminary results have shown [23], the primary structure determination of Dicrocoelium hemoglobin clearly shows conservation of many of the residues involved in the maintenance of the functional properties of hemoglobins and myoglobins from both vertebrate and invertebrate organisms.…”

Section: Amino-acid Composition and Amino And Cauboxyterminal Sequencesmentioning

confidence: 76%

“…In the past few years a number of invertebrate hemoglobins have been isolated and their amino acid sequence determined (G. dibvanchiata [6], Chironomus thummi thummi (CTT-3) [7] and A . limacina [8]). …”

mentioning

confidence: 99%

Isolation and Characterization of the Hemoglobin from the Lanceolate Fluke Dicrocoelium dendriticum

Tuchschmid

Kunz

Wilson

1978

European Journal of Biochemistry

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The hemoglobin of the flatworm Dicrocoelium dendriticum, a lanceolate fluke which infests the hepatic ducts of certain mammals, has been isolated by gel filtration and ion‐exchange chromatography. The molecular weight of the denatured protein was found to be 15500, a value in the same range as hemoglobin subunits. The fact that the native hemoglobin has an apparent molecular weight of 22000 in 0.01 M phosphate buffer, pH 7.4, suggests limited aggregation. The protein contains, as all other myoglobins and hemoglobins, one molecule of non‐covalently associated ferroprotoporphyrin IX per polypeptide chain. It forms the same ligand derivatives with very similar spectral properties as vertebrate hemoglobins. The high oxygen affinity (p50 is 0.07–0.1 mmHg or 9.3–13.3 Pa at 20 °C and pH 7.0) and the absence of heme‐heme interaction (Hill coefficient nH= 1.0) are properties which this heme protein shares with other monomeric hemoglobins from invertebrate and lower vertebrate organisms. The native hemoglobin exists in two forms, having isoelectric points of 4.51 and 4.53, which do not differ in their amino‐acid compositions. Dansylation indicated that the amino‐terminal amino‐acid residue is alanine. The carboxy‐terminal sequence, determined by carboxypeptidase A digestion of the globin, is ‐His‐Ala‐Leu.

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“…However, while a further histidine, the distal histidine-E7, is a t the ligand side of the heme group in sperm whale myoglobin and all other known vertebrate hemoglobins, this residue is in Chironomus hemoglobin a glutamate which makes no heme contact a t all [2] ; on the other hand, in Chironomus hemoglobin there is the isoleucine-Ell which takes over some of the heme contacts of the distal histidine characteristic of the vertebrate myoglobins and hemoglobins [2]. Moreover some other residue is present a t this position in Aplysia myoglobin as it has only one histidine residue [22], probably the proximal histidine. Therefore, results summarized in Table 5 show that no unique role can be arttibuted to the so-called "distal" imidazole in the formation of a stable oxygen * iron complex, which shows that the behaviour of these molecules as oxygen carriers is not uniquely determined by the distal residue, but rather by the polypeptide chain which folds around the heme.…”

Section: Discussionmentioning

confidence: 99%

Functional Properties of Native and Reconstituted Hemoglobins from Chironomus thummi thummi

Amiconi

Antonini

Brunori

et al. 1972

European Journal of Biochemistry

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A procedure for preparation of native globin from Chironomus hemoglobin has been developed and functional properties of native and reconstituted (proto-, meso-and deutero-) hemoglobins have been studied. Globin differs from the corresponding hemoglobin in a number of properties, but the differences are reversible and vanish on addition of protoheme. The oxygen affinity of protohemoglobin ( p l , = 0.7 mm Hg a t 20 "C) is lower than that of meso-and deutero-hemoglobins, respectively, the shape of oxygenation curve of all three hemoproteins being consistent with a simple mass-law formulation. While protohemoglobin shows a small but definite Bohr effect, the oxygen affinity of the deuteroderivative is pH independent. Kinetic results show that binding of oxygen, carbon monoxide and ethylisocyanide to native and reconstituted Chironomus hemoglobins is a simple process, since the association process follows bimolecular behaviour and the dissociation reaction conforms to first-order kinetics.

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Primary structure of aplysia myoglobin: Sequence of a 63‐residue fragment

Cited by 19 publications

References 10 publications

NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements

NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements

Isolation and Characterization of the Hemoglobin from the Lanceolate Fluke Dicrocoelium dendriticum

Functional Properties of Native and Reconstituted Hemoglobins from Chironomus thummi thummi

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