Amino acid sequence of dimeric myoglobin from Cerithidea rhizophorarum

doi:10.1016/0167-4838(83)90166-8

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology

Volume 745, Issue 1, 30 May 1983, Pages 32-36

Biochimica et Biophy...

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Abstract

The complete amino acid sequence of the dimeric myoglobin from Cerithidea rhizophorarum, a common gastropodic mollusc on the Japanese coast having an elongated many-whorled shell, has been determined. The monomer is composed of 151 amino acid residues, is acetylated at the amino terminus, and 75 residues out of 151 are homologous with the monomer of myoglobin from the whelk Busycon canaliculatum. Unlike Aplysia myoglobin, which lacks the distal histidine, Cerithidea myoglobin contains three histidines in its monomer, His-66 being assigned to the distal position, and in its oxymyoglobin form its stability properties show a very strong pH dependence.

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Biochemical characterization of the putative isoforms of myoglobins from mollusks of the Biomphalaria genus
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Citation Excerpt :
The protein is abundant in certain mollusks tissues such as in the radular muscle of Aplysia in which the concentration of myoglobin is two-fold or three-fold higher than that observed in human cardiac and skeletal muscles (Rossi-Fanelli and Antonini, 1957). In gastropods, the presence of myoglobin has been reported either in radular muscle (Takagi et al., 1983; Terwillinger and Read, 1971; Suzuki et al., 2003) or triturative stomach (Suzuki, 1986; Suzuki and Furukohri, 1990). In respect to Biomphalaria genus, myoglobin was described in radular muscle (Dewilde et al., 1998).
Although gastropod myoglobin has been extensively studied, there are knowledge gaps in its biological characteristics. We describe for the first time the presence of a myoglobin in the triturative stomach of Biomphalaria gastropods. We compared biochemical parameters of myoglobins of stomach and radular muscles of Biomphalaria glabrata and Biomphalaria tenagophila. Apomyoglobin and holomyoglobin were obtained. Myoglobin was the most abundant protein in the stomach (85.0%) and radular muscles (80.0%) of the two Biomphalaria species evaluated. The Molecular mass and isoeletric point of stomach myoglobins were 16,124.93 Da and 7.98 and 16.095.28 Da and 7.77 for B. glabrata and B. tenagophila, respectively. Stomach myoglobins of B. glabrata and B. tenagophila rate autoxidation were equal to 8.0 × 10⁻⁴ h⁻¹ ± 0.0002 and 1.0 × 10⁻⁴ h⁻¹ ± 0.00142, respectively. Analysis of N-terminal amino acid sequencing revealed that stomach myoglobins are blocked in this region for a chemical group. Concluding, the differences we observed in the biochemical properties of stomach and radular myoglobins of B. glabrata and B. tenagophila suggest they may be isoform representing an evolutionary event related to the adaptation of these proteins.
Evidence of met-form myoglobin from Theliostyla albicilla radular muscle
2003, International Journal of Biochemistry and Cell Biology
Gastropod mollusc myoglobins provide interesting clues to the evolution of this family of proteins. In addition to conventional monomeric myoglobins, this group also has dimeric and unusual indoleamine dioxygenase-like myoglobins. We isolated myoglobin from the radular muscle of living gastropod mollusc Theliostyla albicilla. The myoglobin appeared to be present in an oxidized met-form, a physiologically inactive form that is not capable of binding oxygen. Under the same extraction conditions, myoglobins mainly of the physiologically active oxy-form have been isolated from other molluscs. The complete amino acid sequence of 157 residues of Theliostyla myoglobin shows that it has a long N-terminal extension of seven residues and contains three functional key residues: CD1-Phe, E7-His, and F8-His. The metmyoglobin can easily be reduced to a ferrous state with Na₂S₂O₄. The autoxidation rate of the oxy-form was comparable to other molluscan myoglobins over a wide pH range, and Theliostyla myoglobin was shown to be stable as an oxygen-binding protein. Thus, the predominantly met-form of myoglobin in Theliostyla can be attributed to the incomplete functioning of the myoglobin reduction system in the radular muscle. Although the function of Theliostyla myoglobin is unclear, it may be a scavenger of H₂O₂.
A myoglobin evolved from indoleamine 2,3-dioxygenase, a tryptophan-degrading enzyme
1998, Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
The distribution, isolation, spectral and oxygen-binding properties, stability of ferrous state (autoxidation), amino acid sequence and gene structure of indoleamine 2,3-dioxygenase (IDO)-like myoglobins are summarized, and their evolution is discussed. Although it has long been thought that all hemoglobins and myoglobins have evolved from a common ancestral gene encoding a 14–16 kDa polypeptide, the discovery of IDO-like myoglobin from several gastropod molluscs clearly indicates that there was an alternative pathway for myoglobin evolution.
Nonvertebrate hemoglobins: Structural bases for reactivity
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The dimer-monomer conversion of Cerithidea myoglobin coupled with the heme iron oxidation
1996, Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
With regard to the distal (E7) residue, gastropod sea mollusc contains both types of myoglobin, one with and the other lacking the distal histidine. We have isolated a myoglobin from the radular muscle of Cerithidea rhizophorarum, a small whelk found on the Japanese coast. Unlike Aplysia myoglobin having a single histidine residue at position 95, Cerithidea myoglobin contains three histidines at positions 48, 66 and 98. Moreover, Cerithidea MbO₂ exists as homodimers and is oxidized, not to the usual form of metMb but to the hemichrome monomers. It was also found that the hemichrome monomers thus produced can easily be converted back to the dimerized oxy-form, if the ferric protein was reduced carefully with a slight excess of sodium hydrosulfite. This dimer-monomer conversion coupled with the heme-iron oxidation in Cerithidea myoglobin is very unique, and the distal histidine at position 66 is probably responsible for its reversible formation of hemichrome from the ferric met-form that occurred transiently in due course of the oxidation reaction of Cerithidea MbO₂
Amino-acid sequence of a cooperative, dimeric myoglobin from the gastropod mollusc, Buccinum undatum L.
1994, Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
The complete amino-acid sequence of a dimeric myoglobin from the radular mussel of the gastropod mollusc, Buccinum undatum L. has been determined. The globin¹, which shows cooperative binding of oxygen, contains 146 amino acids, is N-terminal aminoacetylated, and has histidine residues at position 65 and 97, corresponding to the heme-binding histidines seen in mammalian myoglobins. It shows about 75% and 50% homology, respectively, with the dimeric molluscan myoglobins from Busycon canaliculatum and Cerithidea rhizophorarum, the former of which also shows weak cooperativity, but much less similarity to other species of myoglobin and hemoglobin.

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^☆: Data supplementary to this article are deposited with, and can be obtained from, Elsevier Biomedical Press, B.V., BBA Data Deposition, P.O. Box 1345, 100 BH Amsterdam, The Netherlands. Reference should be made to BBA/DD/253-/31606/745 (1983) 32. The supplementary information includes: amino acid compositions of myoglobin and CNBr- and tryptic peptides; separation and purification by Sephadex G-50 chromatography and HPLC of CNBr-, tryptic and chymotryptic peptides.

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Amino acid sequence of dimeric myoglobin from Cerithidea rhizophorarum☆

Abstract

Biochim. Biophys. Acta

Biochim. Biophys. Acta

FEBS Lett.

J. Biol. Chem.

J. Chromatogr.