Francesco P. Nicoletti

TL;DR: The present spectroscopic investigation supports the notion that HSA could be considered as the prototype of monomeric allosteric proteins.

TL;DR: Interestingly, the triple Tf-trHb mutant bearing only Phe residues in the relevant B10, G8, and CD1 positions is endowed with a higher overall affinity for sulfide characterized by a very fast second-order rate constant and 2 order of magnitude faster kinetics of sulfide release with respect to the wild-type protein.

TL;DR: It is demonstrated that DHP has a unique two-site competitive binding mechanism in which the internal and external binding sites communicate through two conformations of the distal histidine of the enzyme, resulting in nonclassical competitive inhibition.

TL;DR: The two conformations of His55 in equilibrium at room temperature provide a level of control that permits the distal histidine to act as both the acid-base catalyst in the peroxidase mechanism and the stabilizing amino acid for exogenous heme-coordinated ligands.

TL;DR: The allosteric effect of ibuprofen on peroxynitrite isomerization to NO3− catalyzed by ferric human serum heme-albumin (HSA-heme-Fe(III) is reported, highlighting theAllosteric modulation of HSA- heme (III) reactivity by heterotropic interaction(s), and outlining the role of drugs in modulating HSA functions.