Parisa Hosseinzadeha,1, Nicholas M. Marshallb,1, Kelly N. Chacónc,d, Yang Yua, Mark J. Nilgesa,b, Siu Yee Newa,
Stoyan A. Tashkove, Ninian J. Blackburnc, and Yi Lua,b,2
aDepartment of Biochemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801; bDepartment of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801; cInstitute of Environmental and Health, Division of Environmental and Biomolecular Systems, Oregon Health and Science University, Portland, OR 97239; dDepartment of Chemistry, Reed College, Portland, OR 97202; and eDepartment of Nuclear, Plasma, and Radiological Engineering, University of Illinois at Urbana–Champaign, Urbana, IL 61801
http://www.pnas.org/content/113/2/262.full.pdf
aDepartment of Biochemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801; bDepartment of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801; cInstitute of Environmental and Health, Division of Environmental and Biomolecular Systems, Oregon Health and Science University, Portland, OR 97239; dDepartment of Chemistry, Reed College, Portland, OR 97202; and eDepartment of Nuclear, Plasma, and Radiological Engineering, University of Illinois at Urbana–Champaign, Urbana, IL 61801
Abstract
The reduction potential (E°′) is a critical parameter in determining the efficiency of most biological and chemical reactions. Biology employs three classes of metalloproteins to cover the majority of the 2-V range of physiological E°′s. An ultimate test of our under- standing of E°′ is to find out the minimal number of proteins and their variants that can cover this entire range and the structural features responsible for the extreme E°′. We report herein the design of the protein azurin to cover a range from +970 mV to −954 mV vs. standard hydrogen electrode (SHE) by mutating only five residues and using two metal ions. Spectroscopic methods have revealed geometric parameters important for the high E°′. The knowledge gained and the resulting water-soluble redox agents with predictable E°′s, in the same scaffold with the same surface properties, will find wide applications in chemical, bio- chemical, biophysical, and biotechnological fields.
The reduction potential (E°′) is a critical parameter in determining the efficiency of most biological and chemical reactions. Biology employs three classes of metalloproteins to cover the majority of the 2-V range of physiological E°′s. An ultimate test of our under- standing of E°′ is to find out the minimal number of proteins and their variants that can cover this entire range and the structural features responsible for the extreme E°′. We report herein the design of the protein azurin to cover a range from +970 mV to −954 mV vs. standard hydrogen electrode (SHE) by mutating only five residues and using two metal ions. Spectroscopic methods have revealed geometric parameters important for the high E°′. The knowledge gained and the resulting water-soluble redox agents with predictable E°′s, in the same scaffold with the same surface properties, will find wide applications in chemical, bio- chemical, biophysical, and biotechnological fields.
コメント