Abstract
The cytoplasmic hemoglobin II from the gill of the clamLucina pectinata consists of 150 amino acid residues, has a calculatedMm of 17,476, including heme and an acetylated N-terminal residue. It retains the invariant residues Phe 44 at position CD1 and His 65 at the proximal position F8, as well as the highly conserved Trp 15 at position A12 and Pro 38 at position C2. The most likely candidate for the distal residue at position E7, based on the alignment with other globins, is Gln 65. However, optical and EPR spectroscopic studies of the ferri Hb II (Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J.,J. Biol. Chem. 265, 16054–16059, 1990) have implicated a tyrosinate oxygen as the distal ligand. Modeling of theLucina Hb II sequence, using the crystal structure of sperm whale aquometmyoglobin, showed that Tyr 30 substituting for the Leu located at position B10 can place its oxygen within 2.8 Å of the water molecule occupying the distal ligand position. This structural alteration is facilitated by the coordinate mutation of the residue at position CD4, from Phe 46 in the sperm whale myoglobin sequence to Leu 47 inLucina Hb II.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Barnes, R. S. K., Calow, P., and Olive, P. J. W. (1988).The Invertebrates: A New Synthesis, Blackwell Scientific Publications, Oxford, pp. 149–169.
Bashford, D., Chothia, C., and Lesk, A. M. (1987).J. Mol. Biol. 196, 199–216.
Bolognesi, M., Onesti, S., Gatti, G., Coda, A., Ascenzi, P., and Brunori, M. (1989).J. Mol. Biol. 205, 529–544.
Bolognesi, M., Coda, A., Frigerio, F., Gatti, G., Ascenzi, P., and Brunori, M. (1990).J. Mol. Biol. 213, 621–625.
Bolognesi, M., Frigerio, F., Lionetti, C., Rizzi, M., Ascenzi, P., and Brunori, M. (1991). InStructure and Function of Invertebrate Oxygen Carriers (Vinogradov, S. N., and Kapp, O. H., eds.), Springer-Verlag, New York, pp. 163–172.
Bordo, D., and Argos, P. (1990).J. Mol. Biol. 211, 975–988.
Bordo, D., and Argos, P. (1991).J. Mol. Biol. 217, 721–729.
Castor, C. W., Miller, J. W., and Walz, D. A. (1983).Proc. Natl. Acad. Sci. 80, 765–769.
Chan, M. M. S. (1984).Beckman Chromatogr. 5, 2–5.
Connolly, M. L. (1983).Science 221, 709–711.
Crestfield, A. M., Moore, S., and Stein, W. H. (1963).J. Biol. Chem. 238, 622–627.
Egorov, T. A., Kazakov, V. K., Shakhparonov, M. I., and Feigina, M. Yu. (1980).Bioorg. Khim. 6, 349–364.
Gross, E., and Witkop, B. (1962).J. Biol. Chem. 237, 1856–1860.
Henrickson, R. I., and Meredith, S. C. (1984).Anal. Biochem. 136, 65–74.
Kemling, N., Kraus, D. W., Wittenberg, J. B., Vinogradov, S. N., Walz, D. A., Hockenhull-Johnson, J. D., Edwards, B. F. P., and Martin, P. (1991).J. Mol. Biol. (in press).
Konieczny, A., Jensen, E. O., Marcker, K. A., and Legocki, A. B. (1987).Mol. Biol. Rep. 12, 61–66.
Kraus, D. W., and Wittenberg, J. B. (1990).J. Biol. Chem. 265, 16,043–16,053.
Kraus, D. W., Wittenberg, J. B., Lu, J. F., and Peisach, J. (1990).J. Biol. Chem. 265, 16,054–16,059.
Kuriyan, J., Wilz, S., Karplus, M., and Petsko, G. A. (1986).J. Mol. Biol. 192, 133–145.
Lesk, A. M., and Chothia, C. (1980).J. Mol. Biol. 136, 225–270.
Pastore, A., Lesk, A. M., Bolognesi, M., and Onesti, S. (1988).Proteins: Struct. Func. Genet. 4, 240–250.
Read, K. R. H. (1962).Biol. Bull. 123, 605–617.
Read, K. R. H. (1965).Comp. Biochem. Physiol. 15, 137–158.
Read, K. R. H. (1966). InPhysiology of Mollusca (Wilbur, K. M., and Yonge, C. M., eds.), Vol. 2, Academic Press, New York, pp. 209–232.
Suzuki, T., Takagi, T., and Shikama, K. (1981).Biochim. Biophys. Acta 669, 79–83.
Suzuki, T. (1986).J. Biol. Chem. 261, 3692–3699.
Suzuki, T., and Furukohri, T. (1989).Experientia 45, 998–1002.
Suzuki, T., and Furukohri, T. (1990).J. Prot. Chem. 9, 69–73.
Takagi, T., Tobita, M., and Shikama, K. (1983).Biochim. Biophys. Acta 745, 32–36.
Takagi, T., Iida, S., Matsuoka, A., and Shikama, K. (1984).J. Mol. Biol. 180, 1179–1184.
Teale, F. W. J. (1959).Biochim. Biophys. Acta 35, 543.
Tentori, L., Vivaldi, G., Carta, S., Antonini, A., and Brunori, M. (1973).Int. J. Pep. Prot. Res. 5, 182–200.
Terwilliger, R. C., and Terwilliger, N. B. (1985).Comp. Biochem. Physiol. 81B, 255–261.
Walz, D. A., Wider, M. D., Snow, J. W., Dass, C., and Desiderio, D. H. (1988).J. Biol. Chem. 263, 14,189–14,195.
Wellner, D., Pannserselvam, C., and Horecker, B. L. (1990).Proc. Natl. Acad. Sci. 87, 1947–1949.
Wittenberg, J. (1985).Bull. Biol. Soc. Washington 6, 301–310.
Yu, L. P., La Mar, G. N., and Mizukami, H. (1990).Biochemistry 29, 2578–2585.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Hockenhull-Johnson, J.D., Stern, M.S., Martin, P. et al. The amino acid sequence of hemoglobin II from the symbiont-harboring clam Lucina pectinata. J Protein Chem 10, 609–622 (1991). https://doi.org/10.1007/BF01025713
Received:
Published:
Issue Date:
DOI: https://doi.org/10.1007/BF01025713