Utilize este identificador para referenciar este registo: http://hdl.handle.net/10400.1/4338
Título: Redox thermodynamics of low-potential iron-sulfur proteins
Autor: Battistuzzi, Gianantonio
D'Onofrio, Mariapina
Borsari, Marco
Sola, Marco
Macedo, Anjos L.
Moura, José J. G.
Rodrigues, Pedro
Palavras-chave: Ferredoxins
Redox thermodynamics
Electrochemistry
Reduction potential
Data: 2000
Editora: Springer
Citação: Battistuzzi, Gianantonio; D'Onofrio, Mariapina; Borsari, Marco; Sola, Marco; Macedo, Anjos L.; Moura, José J. G.; Rodrigues, Pedro. Redox thermodynamics of low-potential iron-sulfur proteins, Journal of Biological Inorganic Chemistry, 5, 6, 748-760, 2000.
Resumo: The enthalpy and entropy changes associated with protein reduction ( ) were determined for a number of low-potential iron-sulfur proteins through variable temperature direct electrochemical experiments. These data add to previous estimates making available, overall, the reduction thermodynamics for twenty species from various sources containing all the different types of metal centers. These parameters are discussed with reference to structural data and calculated electrostatic metal-environment interaction energies, and redox properties of model complexes. This work, which is the first systematic investigation on the reduction thermodynamics of Fe-S proteins, contributes to the comprehension of the determinants of the differences in reduction potential among different protein families within a novel perspective. Moreover, comparison with analogous data obtained previously for electron transport (ET) metalloproteins with positive reduction potentials, i. e., cytochromes c, blue copper proteins, and HiPIPs, helps our understanding of the factors controlling the reduction potential in ET species containing different metal cofactors. The main result of this work can be summarized as follows. HiPIPs as compares to the low-potential 4Fe Fds is entirely due to enthalpic effects related to the electostatic interactions of the cluster with the proteins matrix and the solvent.
Peer review: yes
URI: http://hdl.handle.net/10400.1/4338
DOI: http://dx.doi.org/10.1007/s007750000164
ISSN: 0949-8257
Aparece nas colecções:CCM2-Artigos (em revistas ou actas indexadas)

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