In this letter we report the first experimental evidence for CO rebinding to human hemoglobin from multiple geminate states. The analysis of the rebinding kinetics using a maximum entropy method allowed the identification of two distinct rebinding states within the protein matrix, which become populated under conditions of increased viscosity in a silica gel at high glycerol concentration. Our findings suggest the presence of at least two distinct docking sites for the photolyzed ligand. Assuming a minimal four-state model, we estimate the microscopic rates and the activation energies for the elementary processes.
Evidence for Two Geminate Rebinding States Following Laser Photolysis of R State Hemoglobin Encapsulated in Wet Silica Gels / Sottini, Silvia; Abbruzzetti, Stefania; Viappiani, Cristiano; Bettati, Stefano; Ronda, Luca; Mozzarelli, Andrea. - In: JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL. - ISSN 1520-6106. - 109:(2005), pp. 11411-11413. [10.1021/jp0514224]
Evidence for Two Geminate Rebinding States Following Laser Photolysis of R State Hemoglobin Encapsulated in Wet Silica Gels
SOTTINI, SILVIA;ABBRUZZETTI, Stefania;VIAPPIANI, Cristiano;BETTATI, Stefano;RONDA, Luca;MOZZARELLI, Andrea
2005-01-01
Abstract
In this letter we report the first experimental evidence for CO rebinding to human hemoglobin from multiple geminate states. The analysis of the rebinding kinetics using a maximum entropy method allowed the identification of two distinct rebinding states within the protein matrix, which become populated under conditions of increased viscosity in a silica gel at high glycerol concentration. Our findings suggest the presence of at least two distinct docking sites for the photolyzed ligand. Assuming a minimal four-state model, we estimate the microscopic rates and the activation energies for the elementary processes.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.