http://www.cnr.it/ontology/cnr/individuo/prodotto/ID207351

Following Ligand Migration Pathways from Picoseconds to Milliseconds in Type II Truncated Hemoglobin from Thermobifida fusca (Articolo in rivista)

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Following Ligand Migration Pathways from Picoseconds to Milliseconds in Type II Truncated Hemoglobin from Thermobifida fusca (Articolo in rivista) (literal)

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Marcelli Agnese [ 1 ] ; Abbruzzetti Stefania [ 2 ] ; Bustamante Juan Pablo [ 3 ] ; Feis Alessandro [ 4 ] ; Bonamore Alessandra [ 5 ] ; Boffi Alberto [ 5 ] ; Gellini Cristina [ 4 ] ; Salvi Pier Remigio [ 4 ] ; Estrin Dario A. [ 3 ] ; Bruno Stefano [ 6 ] ; Viappiani Cristiano [ 2 ] ; Foggi Paolo [ 1,7,8 ] (2012)
Following Ligand Migration Pathways from Picoseconds to Milliseconds in Type II Truncated Hemoglobin from Thermobifida fusca
in PloS one
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Marcelli Agnese [ 1 ] ; Abbruzzetti Stefania [ 2 ] ; Bustamante Juan Pablo [ 3 ] ; Feis Alessandro [ 4 ] ; Bonamore Alessandra [ 5 ] ; Boffi Alberto [ 5 ] ; Gellini Cristina [ 4 ] ; Salvi Pier Remigio [ 4 ] ; Estrin Dario A. [ 3 ] ; Bruno Stefano [ 6 ] ; Viappiani Cristiano [ 2 ] ; Foggi Paolo [ 1,7,8 ] (literal)

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[ 1 ] LENS, European Lab Nonlinear Spect, Florence, Italy [ 2 ] Univ Parma, Dept Phys, I-43100 Parma, Italy [ 3 ] Univ Buenos Aires, Fac Ciencias Exactas & Nat, Dept Quim Inorgan Analit & Quim Fis, INQUIMAE CONICET, Buenos Aires, DF, Argentina [ 4 ] Univ Florence, Dept Chem Ugo Schiff, Florence, Italy [ 5 ] Univ Roma La Sapienza, Dept Biochem Sci, Fdn Cenci Bolognetti, Ist Pasteur, I-00185 Rome, Italy [ 6 ] Univ Parma, Dept Biochem & Mol Biol, I-43100 Parma, Italy [ 7 ] Univ Perugia, Dept Chem, I-06100 Perugia, Italy [ 8 ] INO CNR, Florence, Italy (literal)

Titolo

Following Ligand Migration Pathways from Picoseconds to Milliseconds in Type II Truncated Hemoglobin from Thermobifida fusca (literal)

Abstract

CO recombination kinetics has been investigated in the type II truncated hemoglobin from Thermobifida fusca (Tf-trHb) over more than 10 time decades (from 1 ps to similar to 100 ms) by combining femtosecond transient absorption, nanosecond laser flash photolysis and optoacoustic spectroscopy. Photolysis is followed by a rapid geminate recombination with a time constant of similar to 2 ns representing almost 60% of the overall reaction. An additional, small amplitude geminate recombination was identified at similar to 100 ns. Finally, CO pressure dependent measurements brought out the presence of two transient species in the second order rebinding phase, with time constants ranging from similar to 3 to similar to 100 ms. The available experimental evidence suggests that the two transients are due to the presence of two conformations which do not interconvert within the time frame of the experiment. Computational studies revealed that the plasticity of protein structure is able to define a branched pathway connecting the ligand binding site and the solvent. This allowed to build a kinetic model capable of describing the complete time course of the CO rebinding kinetics to Tf-trHb. (literal)

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