Following ligand migration pathways from picoseconds to milliseconds in type ii truncated hemoglobin from thermobifida fusca

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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 ~100 ms) by combining femtosecond transient absorption, nanosecond laser flash photolysis and optoacoustic spectroscopy. Photolysis is fo...

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Detalles Bibliográficos
Autores principales: Marcelli, A., Abbruzzetti, S., Bustamante, J.P., Feis, A., Bonamore, A., Boffi, A., Gellini, C., Salvi, P.R., Estrin, D.A., Bruno, S., Viappiani, C., Foggi, P.
Formato: Artículo publishedVersion
Lenguaje:Inglés
Publicado: 2012
Materias:
carbon monoxide
truncated hemoglobin
article
bacterium
binding affinity
binding kinetics
binding site
complex formation
controlled study
enthalpy
entropy
ligand binding
molecular dynamics
molecular recognition
nonhuman
photoacoustic spectroscopy
photolysis
protein binding
quantum yield
steady state
temperature sensitivity
Thermobifida fusca
Actinomycetales
Carbon Monoxide
Kinetics
Ligands
Photolysis
Protein Binding
Time Factors
Truncated Hemoglobins
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_19326203_v7_n7_p_Marcelli
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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