Design of a single protein that spans the entire 2-V range of physiological redox potentials

The reduction potential (Eo′) 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 Eo′s. An ultimate test of our understanding of Eo′ is to find out th...

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Published inProceedings of the National Academy of Sciences - PNAS Vol. 113; no. 2; pp. 262 - 267
Main Authors Hosseinzadeh, Parisa, Marshall, Nicholas M., Chacón, Kelly N., Yu, Yang, Nilges, Mark J., New, Siu Yee, Tashkov, Stoyan A., Blackburn, Ninian J., Lu, Yi
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 12.01.2016
National Acad Sciences
SeriesFrom the Cover
Subjects
Azurin - chemistry
Azurin - metabolism
Bacterial proteins
Biochemistry
Biophysics
Biotechnology
Electrochemical Techniques
Electron Spin Resonance Spectroscopy
Gram-positive bacteria
Models, Molecular
Mutation - genetics
Oxidation-Reduction
Physical Sciences
Physiology
Protein Engineering
Spectrometry, X-Ray Emission
Spectrophotometry, Ultraviolet
Spectrum analysis
secondary coordination sphere
cupredoxins
electron transfer
reduction potential
azurin
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Abstract The reduction potential (Eo′) 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 Eo′s. An ultimate test of our understanding of Eo′ 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 Eo′. 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 Eo′. The knowledge gained and the resulting water-soluble redox agents with predictable Eo′s, in the same scaffold with the same surface properties, will find wide applications in chemical, biochemical, biophysical, and biotechnological fields.
AbstractList 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 understanding 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, biochemical, biophysical, and biotechnological fields. (ProQuest: ... denotes formulae/symbols omitted.)
The reduction potential (Eo′) 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 Eo′s. An ultimate test of our understanding of Eo′ 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 Eo′. 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 Eo′. The knowledge gained and the resulting water-soluble redox agents with predictable Eo′s, in the same scaffold with the same surface properties, will find wide applications in chemical, biochemical, biophysical, and biotechnological fields.
Nature spent millions of years to evolve electron transfer proteins that span a wide range of reduction potentials (E°′) under physiological conditions, from −1 V to 1 V vs. standard hydrogen electrode. Understanding the rules that govern such tuning within similar classes of metalloproteins enables scientists to rationally tune the E°′of their catalysts without changing the active site. An ultimate test of such understanding is to achieve the entire range of E°′ within a single protein, a feat that has not been achieved yet. Herein, we conclusively found that we can cover the entire 2-V range of E°′ using a single protein with five mutations and two metal ions. We have also provided explanations for structural features responsible for such high potential. 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 understanding 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, biochemical, 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 understanding 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, biochemical, biophysical, and biotechnological fields.
Author Yu, Yang
Tashkov, Stoyan A.
Blackburn, Ninian J.
Marshall, Nicholas M.
Lu, Yi
Hosseinzadeh, Parisa
New, Siu Yee
Chacón, Kelly N.
Nilges, Mark J.
Author_xml – sequence: 1
  givenname: Parisa
  surname: Hosseinzadeh
  fullname: Hosseinzadeh, Parisa
  organization: Department of Biochemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801
– sequence: 2
  givenname: Nicholas M.
  surname: Marshall
  fullname: Marshall, Nicholas M.
  organization: Department of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801
– sequence: 3
  givenname: Kelly N.
  surname: Chacón
  fullname: Chacón, Kelly N.
  organization: Institute of Environmental and Health, Division of Environmental and Biomolecular Systems, Oregon Health and Science University, Portland, OR 97239
– sequence: 4
  givenname: Yang
  surname: Yu
  fullname: Yu, Yang
  organization: Department of Biochemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801
– sequence: 5
  givenname: Mark J.
  surname: Nilges
  fullname: Nilges, Mark J.
  organization: Department of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801
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  givenname: Siu Yee
  surname: New
  fullname: New, Siu Yee
  organization: Department of Biochemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801
– sequence: 7
  givenname: Stoyan A.
  surname: Tashkov
  fullname: Tashkov, Stoyan A.
  organization: Department of Nuclear, Plasma, and Radiological Engineering, University of Illinois at Urbana–Champaign, Urbana, IL 61801
– sequence: 8
  givenname: Ninian J.
  surname: Blackburn
  fullname: Blackburn, Ninian J.
  organization: Institute of Environmental and Health, Division of Environmental and Biomolecular Systems, Oregon Health and Science University, Portland, OR 97239
– sequence: 9
  givenname: Yi
  surname: Lu
  fullname: Lu, Yi
  organization: Department of Chemistry, University of Illinois at Urbana–Champaign, Urbana, IL 61801
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Keywords secondary coordination sphere
cupredoxins
electron transfer
reduction potential
azurin
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1P.H. and N.M.M. contributed equally to this work.
Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA, and approved October 21, 2015 (received for review August 10, 2015)
Author contributions: P.H., N.M.M., and Y.L. designed research; P.H., N.M.M., K.N.C., Y.Y., S.Y.N., and S.A.T. performed research; P.H., N.M.M., K.N.C., M.J.N., N.J.B., and Y.L. analyzed data; and P.H., N.M.M., and Y.L. wrote the paper.
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Snippet The reduction potential (Eo′) is a critical parameter in determining the efficiency of most biological and chemical reactions. Biology employs three classes of...
The reduction potential (E°') is a critical parameter in determining the efficiency of most biological and chemical reactions. Biology employs three classes of...
Nature spent millions of years to evolve electron transfer proteins that span a wide range of reduction potentials (E°′) under physiological conditions, from...
The reduction potential (E...') is a critical parameter in determining the efficiency of most biological and chemical reactions. Biology employs three classes...
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SubjectTerms Azurin - chemistry
Azurin - metabolism
Bacterial proteins
Biochemistry
Biophysics
Biotechnology
Electrochemical Techniques
Electron Spin Resonance Spectroscopy
Gram-positive bacteria
Models, Molecular
Mutation - genetics
Oxidation-Reduction
Physical Sciences
Physiology
Protein Engineering
Spectrometry, X-Ray Emission
Spectrophotometry, Ultraviolet
Spectrum analysis
Title Design of a single protein that spans the entire 2-V range of physiological redox potentials
URI https://www.jstor.org/stable/26467347
http://www.pnas.org/content/113/2/262.abstract
https://www.ncbi.nlm.nih.gov/pubmed/26631748
https://www.proquest.com/docview/1759028730
https://search.proquest.com/docview/1760854502
https://pubmed.ncbi.nlm.nih.gov/PMC4720346
Volume 113
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