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Abstract
We describe a simple method for the determination of heme protein reduction potentials. We use the method to determine the reduction potentials for the PAS-A domains of the regulatory heme proteins human NPAS2 (Em=−115mV±2mV, pH 7.0) and human CLOCK (Em=−111mV±2mV, pH 7.0). We suggest that the method can be easily and routinely applied to the determination of reduction potentials across the family of heme proteins.
Highlights
Heme-containing proteins form a vast and biologically important superfamily: they are found in all living species and carry out a very wide array of functions
An important property of the heme group is the redox behavior of the metal, which can exist in +2, +3 or +4 oxidation states
In 1991, Massey published what was described as a simple method for the determination of redox potentials [31]
Summary
Heme-containing proteins form a vast and biologically important superfamily: they are found in all living species and carry out a very wide array of functions. Beyond the scope of these ‘traditional’ heme proteins, there is clear evidence of a wider regulatory role for heme in biological systems; examples include roles for heme in ion channel regulation, transcriptional control and gas sensing, but these roles are as yet only poorly defined at a structural, mechanistic and functional level. Across the entire family of heme proteins, the stability of individual iron oxidation states can vary enormously as a complex function of different variables including the nature, orientation and hydrogen bonding interactions of the heme ligand(s), the identity of active site residues around the heme group, solvent accessibility, the heme substituents, the orientation of the heme group and vinyl.
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