Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 2, Pages 262-267Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1515897112
Keywords
reduction potential; secondary coordination sphere; azurin; electron transfer; cupredoxins
Categories
Funding
- US National Science Foundation [CHE 14-13328]
- US National Institutes of Health [NIH R01GM054803]
- National Science Foundation Graduate Research Fellowship [DGE-0925180]
- US Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- National Institutes of Health
- National Institute of General Medical Sciences [P41GM103393]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1413328] Funding Source: National Science Foundation
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The reduction potential (E degrees') 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 degrees's. An ultimate test of our understanding of E degrees' 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 degrees'. 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 degrees'. The knowledge gained and the resulting water-soluble redox agents with predictable E degrees's, in the same scaffold with the same surface properties, will find wide applications in chemical, biochemical, biophysical, and biotechnological fields.
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