Development of a heme protein structure-electrochemical function database.
Proteins containing heme, iron(protoporphyrin IX) and its variants, continue to be one of the most-studied classes of biomolecules due to their diverse range of biological functions. The literature is abundant with reports of structural and functional characterization of individual heme proteins which demonstrate that heme protein reduction potential values, E(m), span the range from -550 mV to +450 mV versus SHE. In order to unite these data for the purposes of global analysis, a new web-based resource of heme protein structure-function relationships is presented: the Heme Protein Database (HPD). This database is the first of its kind to combine heme protein structural classifications including protein fold, heme type and heme axial ligands, with heme protein reduction potential values in a web-searchable format. The HPD is located at http://heme.chem.columbia.edu/heme.php. The data illustrate that heme protein E(m) values are modulated over a 300 mV range by the type of global protein fold, a 600 mV range by the type of porphyrin and an 800 mV range by the axial ligands. Thus, the 1 V range observed in heme protein reduction potential values in biological systems arises from subtle combinations of these various factors.
Reedy
Charles J
CJ
Department of Chemistry, Columbia University, 3000 Broadway, MC 3121, New York, NY 10027, USA.
Elvekrog
Margaret M
MM
Gibney
Brian R
BR
D030562:Databases, Protein; D004563:Electrochemistry; D006420:Hemeproteins / Q000737:chemistry*; D020407:Internet; D008024:Ligands; D010084:Oxidation-Reduction; D013816:Thermodynamics
D006420:Hemeproteins; D008024:Ligands