Physicochemical and structural properties of the extracellular haemoglobin of Ophelia bicornis

Mezzasalma, Valerio; Stefano, L. Di; Piazzese, Santo; Zagra, Michela; Salvato, Benedetto; Tognon, Giuseppe; Ghiretti‐Magaldi, Anna

doi:10.1016/0167-4838(85)90181-5

Cited by 18 publications

(4 citation statements)

References 25 publications

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“…While the presence of an extracellular Hb in the polychaete Ophelia bicornis has been described previously [14], in the present paper, we demonstrate, for the first time, the presence of a Mb in the body wall of this species. The structure, the physicochemical characteristics and the functional properties of the Mb are described and discussed in comparison with Mbs from other invertebrates.…”

Section: Introductionsupporting

confidence: 82%

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Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis

Sanna¹,

Manconi²,

Castagnola

et al. 2005

Biochemical Journal

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The myoglobin of the polychaete annelid Ophelia bicornis was isolated, purified to homogeneity and characterized. The primary structure, obtained from cDNA and protein sequencing, consists of 139 amino acid residues. The alignment with other globin sequences showed that O. bicornis myoglobin misses the pre-A helix and the first six residues of the A helix. The presence of a PheB10-GlnE7 haem distal residue pair is in agreement with the measured oxygen affinity (P50=0.85 mmHg; 1 mmHg=0.133 kPa) and the only slightly higher autoxidation rate constant (0.28 h(-1)) with respect to that of the sperm whale myoglobin mutant E7 His-->Gln (0.21 h(-1)) and to elephant myoglobin (0.1 h(-1)). Oxygen-binding co-operativity was found to be absent under all the examined experimental conditions. The resistance of O. bicornis myoglobin towards autoxidation seems to confirm the important role of part of the A helix in the stability of the globin. The higher pKa of the acid-alkaline ferric transition of O. bicornis with respect to Asian elephant myoglobin, as well as the higher absorbance ratio of its ferric form to the oxy form measured in the Soret region (gammamet/gammaoxy) with respect to that of the African elephant myoglobin, suggested a stronger interaction between the distal glutamine and the water molecule at the sixth co-ordinate position.

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Section: Introductionsupporting

confidence: 82%

“…[35], it is not surprising that the oxygen-binding properties of this globin are compatible with an oxygen-storage function, also considering the presence of a giant Hb freely dissolved in the haemolymph [14].…”

Section: Figure 10 Oxygen-binding Curve Of O Bicornis Mbmentioning

confidence: 99%

Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis

Sanna¹,

Manconi²,

Castagnola

et al. 2005

Biochemical Journal

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“…However, the composition of this central subunit would be different from that of the other one-twelfth subunits as suggested by ESI-MS stoichiometry and it could be made up of four trimers (2 T1 and 2 T2) although alternative compositions may be possible. The presence of a thirteenth subunit located at the center of Arenicola HBL Hb has never been observed before, but two papers men- [52][53][54][55], Glossoscolex paulistus [48], Eophila tellinii 1.561, Oenoize ,fulgida [57] and Euzonus mucronatcz [%I.…”

Section: Discussionmentioning

confidence: 99%

Quaternary Structure of the Extracellular Haemoglobin of the Lugworm Arenicola marina

Zal

Green²,

Lallier

et al. 1997

European Journal of Biochemistry

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To elucidate the quaternary structure of the extracellular haemoglobin (Hb) of the marine polychaete Arenicola marina (lugworm) it was subjected to multi-angle laser-light scattering (MALLS) and to electrospray-ionisation mass spectrometry (ESI-MS). It was also subjected to SDS/PAGE analysis for comparative purposes. MALLS analysis gave a molecular mass of 3648 % 24 kDa and a gyration radius of 11.3 rt 1.7 nm. Maximum entropy analysis of the multiply charged electrospray spectra of the native, dehaemed, reduced and carbamidomethylated Hb forms, provided its complete polypeptide chain and subunit composition. We found, in the reduced condition, eight globin chains of molecular masses 15952. Keywords: Arenicola ; haemoglobin ; quaternary structure ; multi-angle laser-light scattering; electrospray mass spectrometry.The giant extracellular haemoglobins (Hb) and chlorocruorins found in annelids [1] and vestimentiferans [2, 31 are characterised by an acidic isoelectric point and by an hexagonal symmetry in electron micrographs consisting of two superimposed hexagonal arrays of twelve spherical subunits, the hexagonal bilayer (HBL). These HBL Hb also contain a low haem and iron contents (about 67% of those observed in other Hbs) and consist of two types of chains, globin chains (~1 6 -1 8 kDa), accounting for approximately 70% of the total mass, and haem-deficient linker chains (~2 4 -2 8 kDa) necessary for the assemblage into the HBL structure [1,. The intertidal marine polychaete Arenicola marina (L.) was one of the first 60s (~3 6 0 0 kDa)

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“…With kind permission by La Recherche. Bannister, Bannister, and Anastasi, 1976 The hexagon center is generally devoid of subunits and was constituted by a hole of about 7-8 nm diameter; however, some annelid EHbs were shown to possess a central subunit, such as Oenone fulgida (Van Bruggen and Weber, 1974), Nepthys hombergii (Wells and Dales, 1976), Nepthys incisa (Wells and Dales, 1976;Messerschmidt et al, 1983;Vinogradov and Kapp, 1983), Ophelia bicornis Mezzasalma et al, 1985;Cejka et al, 1991Cejka et al, , 1992, Maoridrilus montanus (Ellerton et al, 1987), Glossoscolex paulistus (El Idrissi Slitine, Torriani, and Vachette, 1990), Eophila tellinii (Cejka et al, 1989), Euzonus mucronata (Terwilliger et al, 1977b), and Arenicola marina (Zal et al, 1997a(Zal et al, , 1997b (Figure 16.3). The existence of a central subunit suggested that this was similar or equivalent to another one-twelfth of the native molecule, although to date no central subunit has been isolated and/or characterized.…”

Section: Architecturementioning

confidence: 99%

Extracellular Hemoglobins from Annelids, and their Potential Use in Biotechnology

Zal

Rousselot

2014

Outstanding Marine Molecules

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Physicochemical and structural properties of the extracellular haemoglobin of Ophelia bicornis

Cited by 18 publications

References 25 publications

Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis

Functional and structural characterization of the myoglobin from the polychaete Ophelia bicornis

Quaternary Structure of the Extracellular Haemoglobin of the Lugworm Arenicola marina

Extracellular Hemoglobins from Annelids, and their Potential Use in Biotechnology

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