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.
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.
|Accession ID:||UniProt: B3EWN9; PDB ID: 4AZU|
|Source:||Expressed and purified from E. coli|
|Molecular Weight:||13,886 kDa|
|Amino Acid Sequence:||AECSVDIQGNDQMQFNTNAITVDKSCKQFTVNLSHPGNLPKNVMGHNWVLSTAADMQGVVTDGMASGLDKDYLKPDDSRVIAHTKLIGSGEKDSVTFDVSKLKEGEQYMSFCTFPGHSALMKGTLTLK|
|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|
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