Faculty Advisor

Arguello, Jose' M.


Cu+ATPases are vital membrane proteins that utilize hydrolysis of ATP to transport Cu+ ions into the periplasm. While the ATPase mechanisms are understood, studies of the interactions with chaperone proteins are still incomplete. The goal of this MQP is to understand copper partitioning in the periplasm and identify periplasmic partners of Cu-ATPases in P. aeruginosa. Protocols for Cu+ determination in subcellular protein fractions, Cu+ sensitivity, cytochrome c oxidase and Cu2+ reductase activity assays were optimized. Assays involving mutant ΔcopA1 and ΔcopA2 strains showed evidence of altered Cu+ homeostasis, but showed no clear results on Cu2+ reductase activity or interactions with periplasmic Cu+ chaperones. These findings were reported in Metallomics (2013) (2):144-151.


Worcester Polytechnic Institute

Date Accepted

March 2013


Biology and Biotechnology

Project Type

Major Qualifying Project



Advisor Department

Chemistry and Biochemistry