Enthalpy/entropy compensation phenomena in the reduction thermodynamics of electron transport metalloproteins.
Compensation phenomena between the enthalpy and entropy changes of the reduction reaction for all classes of electron transport metalloproteins, namely cytochromes, iron-sulfur, and blue copper proteins, are brought to light. This is the first comprehensive report on such effects for biological redox reactions. Following Grunwald's approach for the interpretation of H/ S compensation for solution reactions, it is concluded that reduction-induced solvent reorganization effects involving the hydration shell of the molecule dominate the reduction thermodynamics in these species, although they have no net effect on the E degrees values, owing to exact compensation. Thus the reduction potentials of these species are primarily determined by the selective enthalpic stabilization of one of the two oxidation states due to ligand binding interactions and electrostatics at the metal site and by the entropic effects of reduction-induced changes in protein flexibility.
Department of Chemistry, University of Modena and Reggio Emilia, via Campi 183, 41100, Modena, Italy.
Gianantonio
G
Battistuzzi
Marco
M
Borsari
Giulia
G
Di Rocco
Antonio
A
Ranieri
Marco
M
Sola
D001400:Azurin / Q000737:chemistry; D001426:Bacterial Proteins; D045304:Cytochromes c / Q000737:chemistry; D004579:Electron Transport; D019277:Entropy; D005288:Ferredoxins / Q000737:chemistry; D007506:Iron-Sulfur Proteins / Q000737:chemistry; D008667:Metalloproteins / Q000737:chemistry*; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry; D012416:Rubredoxins / Q000737:chemistry; D013816:Thermodynamics
C081714:2Fe-2S ferredoxin; D001426:Bacterial Proteins; D005288:Ferredoxins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D045322:Photosynthetic Reaction Center Complex Proteins; D012416:Rubredoxins; C007943:high potential iron-sulfur protein; D001400:Azurin; D045304:Cytochromes c