S-Sulfohemoglobin and disulfide exchange: the mechanisms of sulfide binding by Riftia pachyptila hemoglobins.

@article{Zal1998SSulfohemoglobinAD,
  title={S-Sulfohemoglobin and disulfide exchange: the mechanisms of sulfide binding by Riftia pachyptila hemoglobins.},
  author={Franck Zal and Emmanuelle Leize and François H. Lallier and Andr{\'e} Toulmond and Alain van Dorsselaer and James J. Childress},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 15},
  pages={8997-9002}
}
The deep sea hydrothermal tube worm Riftia pachyptila possesses a multihemoglobin system with three different extracellular hemoglobins (Hbs; V1, V2, and C1): two dissolved in the vascular blood, V1 and V2, and one in the coelomic fluid, C1. V1 consists of four heme-containing chains and four linker chains. The globin chains making up V2 and C1 are, with one exception, common to V1. Remarkably these Hbs are able to bind oxygen and sulfide simultaneously and reversibly at two different sites… CONTINUE READING