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The Evolution of Hemocyanin
Author(s) -
Schuld Molly,
Bhatia Rohit,
Bobber Summer,
Dorava Benjamin,
Fragoso Brandon,
Johanneck Olivia,
Ledger Kiley,
Haralson Brenden Mclaughlin,
Mitchell Alex,
Perez Jonathan,
Rivera Tiffany,
Ruiz Julian,
Sheikh Samia,
Ya Ahyu,
Perez Jose
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.751.5
Subject(s) - hemocyanin , hemoglobin , limulus , oxygen transport , bohr effect , oxygen , biology , biophysics , evolutionary biology , ecology , zoology , chemistry , biochemistry , oxygen–haemoglobin dissociation curve , genetics , organic chemistry , antigen
Hemocyanin is the oxygen‐carrying protein in most mollusks and some arthropods. It is relevant to the study of natural selection as it evolved after hemoglobin. How do environmental factors affect the structure and the oxygen affinity of hemoglobin compared to the structure and the oxygen affinity of hemocyanin? The Ronald Reagan High School MAPS Team used 3‐D modeling and printing technology to examine the structural differences that affect oxygen affinity of hemocyanin and hemoglobin under various environmental conditions. Specifically, research was focused on hemocyanin of Limulus polyphemus (Atlantic horseshoe crab) and hemoglobin of Scapharca inaequivalvis (Ark clam). Temperature affects the affinity of both hemocyanin and hemoglobin for oxygen. The partial pressure of CO2, pH, the concentration of 2,3‐DPG, and the presence of unusual hemoglobin species, and temperature are all physiological factors that may influence the oxygen affinity of hemoglobin and hemocyanin. The study of evolution of a particular protein is important to our understanding of its function. By studying the variations that were selected for in hemocyanin as it evolved from hemoglobin through comparison of both protein structures, a better grasp of the evolutionary process can be developed. In an ongoing scientific study, hemocyanin is being extracted from species and being inserted into other species that utilize hemoglobin, testing the potential benefits of hemocyanin. Our protein story and physical models defining the similarities and differences in hemoglobin and hemocyanin structure offer insight into their similar, but unique, functions. Support or Funding Information The MAPS program is supported by the Center for BioMolecular Modeling at the Milwaukee School of Engineering.