Metal binding specificity in myohemerythrin
Chemistry, Dr. Russell
In the student's own words:
I think the best part of doing research at Gustavus is becoming familiar with the working environment on campus. I know where to find different machines and instruments and how to use them. I think this gives me a confidence and independence in the lab and in my own work. Going to lab is no longer a stressful few hours one day a week, but rather something I know I can do successfully 5 days a week. I think doing research helps you think more like a professional, and less like a student.
Myohemerythrin (myoHr) is an oxygen transport protein containing a di-iron active site found in Phascolopsis gouldii. Metalloprotein II is a di-cadmium transport protein found in Nereis diversicolor with 80.8% identity with myoHr. This makes MP II an unusual protein for cadmium binding, a metal considered as waste in most biological systems. MyoHr is not found in nature with bound cadmium. Separate iron and cadmium incorporations of myoHr were performed on unfolded apoprotein to assess the ability of myoHr to bind Cd2+. Ultraviolet-visible spectroscopy detected successful incorporations of both Fe2+ and Cd2+. MyoHr is not found with cadmium bound in nature presumably because it has a higher affinity for iron than cadmium.
This research was supported by the 2007 Greater Gustavus Summer Research Fund.
More student thoughts:
Watching your peers present their research brings an appreciation of different areas of science. They have a chance to explain what they're studying and interest you in something you've never thought of.