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An enzymatic globin from a marine worm

Author

Listed:
  • Lukasz Lebioda

    (University of South Carolina)

  • Michael W. LaCount

    (University of South Carolina)

  • Erli Zhang

    (University of South Carolina
    Parke-Davis Pharmaceutical Research)

  • Yung Pin Chen

    (University of South Carolina)

  • Kaiping Han

    (University of South Carolina)

  • Margaret M. Whitton

    (Parke-Davis Pharmaceutical Research)

  • David E. Lincoln

    (University of South Carolina)

  • Sarah A. Woodin

    (University of South Carolina)

Abstract

Some marine worms, such as Thelepus crispus and Notomastus lobatus, secrete brominated aromatic molecules and other halogenated metabolites as repellants1. Other species, such as Amphitrite ornata, do not produce repellants but are adapted to the chemical warfare of N. lobatus and cohabit with them in estuarine mudflats. The halocompounds are tolerated by A. ornata as they are degraded by dehaloperoxidase (DHP)2. We have determined the amino-acid sequence and crystal structure of DHP and find that its fold is typical of the globin family, indicating that the enzyme evolved from an oxygen carrier protein. Residues at the dimer interface do not correspond to those in tetrameric and dimeric haemoglobins and the spatial arrangement of the dimers is different. The complete amino-acid sequence is most similar to that of myoglobin from the sea hare, with 20.6% identity among 126 overlapping amino acids.

Suggested Citation

  • Lukasz Lebioda & Michael W. LaCount & Erli Zhang & Yung Pin Chen & Kaiping Han & Margaret M. Whitton & David E. Lincoln & Sarah A. Woodin, 1999. "An enzymatic globin from a marine worm," Nature, Nature, vol. 401(6752), pages 445-445, September.
    • Handle: RePEc:nat:nature:v:401:y:1999:i:6752:d:10.1038_46728
    DOI: 10.1038/46728
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