Redox Potential-Tuned Azurin Proteins
Azurin proteins with redox potentials that span the entire range of physiological redox potentials (from -950 mV to + 972 mV vs. standard hydrogen electrode) that can be used as tunable and water soluble redox agents for biochemical and biophysical studies.
Highlights:
- Highly pure, Pseudomonas aeruginosa azurin expressed in and purified from Escherichia coli
- Display a wide range of reduction potentials from -954 to +972 mV (+/-10 mV) vs. SHE (the variants with negative reduction potentials are not stable in their reductive form)
- Water soluble and relatively stable in organic solvents
- Possess same overall structure and surface properties of native azurin and contain either a Cu center (as in azurin) or Ni in the place of the Cu center
Redox reactions are at the heart of numerous biological functions and chemical transformations, from electron transfer (ET) in photosynthesis and respiration to catalytic activations of C-H bonds and other molecules. The redox potential (E°) is one of the most important parameter in determining the efficiency of reactions. In contrast to a number of redox agents that are soluble in organic solvent, there are very few water-soluble/stable chemical redox agents within the physiological E°′ range. Even for those redox agents that can cover a wide range of E°′ in nonaqueous solutions, combining different redox agents with different scaffolds or surface properties makes it difficult to carry out systematic studies of the effect of E°′ on ET or catalytic functions, as it is difficult to deconvolute different factors in the redox process.
From the laboratory of Yi Lu, PhD, University of Illinois at Urbana-Champaign.
Azurin proteins with redox potentials that span the entire range of physiological redox potentials (from -950 mV to + 972 mV vs. standard hydrogen electrode) that can be used as tunable and water soluble redox agents for biochemical and biophysical studies.
Highlights:
- Highly pure, Pseudomonas aeruginosa azurin expressed in and purified from Escherichia coli
- Display a wide range of reduction potentials from -954 to +972 mV (+/-10 mV) vs. SHE (the variants with negative reduction potentials are not stable in their reductive form)
- Water soluble and relatively stable in organic solvents
- Possess same overall structure and surface properties of native azurin and contain either a Cu center (as in azurin) or Ni in the place of the Cu center
Redox reactions are at the heart of numerous biological functions and chemical transformations, from electron transfer (ET) in photosynthesis and respiration to catalytic activations of C-H bonds and other molecules. The redox potential (E°) is one of the most important parameter in determining the efficiency of reactions. In contrast to a number of redox agents that are soluble in organic solvent, there are very few water-soluble/stable chemical redox agents within the physiological E°′ range. Even for those redox agents that can cover a wide range of E°′ in nonaqueous solutions, combining different redox agents with different scaffolds or surface properties makes it difficult to carry out systematic studies of the effect of E°′ on ET or catalytic functions, as it is difficult to deconvolute different factors in the redox process.
From the laboratory of Yi Lu, PhD, University of Illinois at Urbana-Champaign.
| Catalog Number | Product | DataSheet | Size | AVAILABILITY | Price | Qty |
|---|
| Product Type: | Protein |
| Name: | Azurin (Az) |
| Accession ID: | B3EWN9 |
| Source: | Expressed and purified from E. coli |
| Molecular Weight: | 13,886 kDa |
| Amino Acid Sequence: | AECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSKLKEGEQYMSFCTFPGHSALMKGTLTLK |
| Fusion Tag(s): | None |
| Purity: | >95% |
| Buffer: | Usually ammonium acetate |
| Concentration: | Varies by protein (0.01-5 mM); see individual product label for details |
| Activity: | Redox agents with wide range of potentials |
| Suggested Amount per Experiment: | Depends on experiment. Usually few µL of 0.1 mM |
| Comments: | Contains a Cu- or Ni-binding site |
| Storage: | -80C, Can be kept at 4C if used within a month |
| Shipped: | Dry ice |
- Hosseinzadeh P, Marshall NM, Chacón KN, Yu Y, Nilges MJ, New SY, Tashkov SA, Blackburn NJ, Lu Y. Design of a single protein that spans the entire 2-V range of physiological redox potentials. Proc Natl Acad Sci U S A. 2016 Jan 12;113(2):262-7.
- Marshall NM, Garner DK, Wilson TD, Gao YG, Robinson H, Nilges MJ, Lu Y. Rationally tuning the reduction potential of a single cupredoxin beyond the natural range. Nature. 2009 Nov 5;462(7269):113-6.
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