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A comparative kinetic analysis of the reactivity of plant, horse, and human respiratory cytochrome c towards cytochrome c oxidase

AuthorsRodríguez-Roldán, Vicente ; García-Heredia, José M. ; Navarro, José A. ; Hervás, Manuel ; Cerda, Berta de la ; Molina-Heredia, Fernando P. ; Rosa, Miguel A. de la
Cytochrome c
Cytochrome c oxidase
Laser flash spectroscopy
Kinetic analysis
Issue Date12-Jun-2006
CitationBiochemical and Biophysical Research Communications 346(3): 1108-1113 (2006)
AbstractTwo synthetic genes coding for human and Arabidopsis cytochrome c, respectively, have been designed and constructed, and the recombinant proteins have been over-expressed in Escherichia coli cells. Thus a comparative analysis of the two heme proteins, including horse cytochrome c as a reference, has been performed. In addition to their physico-chemical properties, the redox behavior of the three proteins has been analyzed by following the kinetics of both their reduction by flavin semiquinones (lumiflavin, riboflavin, and FMN) and oxidation by cytochrome c oxidase. The resulting data indicate that the accessibility and electrostatic charge of the active site do not differ in a significant way among the three proteins, but human cytochrome c exhibits some intriguing differences when interacting with cytochrome c oxidase that could be related to the amino acid changes underwent by the latter along evolution.
Description6 pages, 2 figures, 3 tables.-- PMID: 16782050 [PubMed].-- Printed version published on Aug 4, 2006.
Publisher version (URL)http://dx.doi.org/10.1016/j.bbrc.2006.06.022
Appears in Collections:(IBVF) Artículos
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