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Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases

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Abstract

In this work we present a kinetic study of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and members of the three different classes of superoxide reductases (SORs). SORs from the sulfate-reducing bacteria Desulfovibrio vulgaris (Dv) and D. gigas (Dg) were chosen as prototypes of classes I and II, respectively, while SOR from the syphilis spyrochete Treponema pallidum (Tp) was representative of class III. Our results show evidence for different behaviors of SORs toward electron acceptance, with a trend to specificity for the electron donor and acceptor from the same organism. Comparison of the different k app values, 176.9±25.0 min−1 in the case of the Tp/Tp electron transfer, 31.8±3.6 min−1 for the Dg/Dg electron transfer, and 6.9±1.3 min−1 for Dv/Dv, could suggest an adaptation of the superoxide-mediated electron transfer efficiency to various environmental conditions. We also demonstrate that, in Dg, another iron–sulfur protein, a desulforedoxin, is able to transfer electrons to SOR more efficiently than rubredoxin, with a k app value of 108.8±12.0 min−1, and was then assigned as the potential physiological electron donor in this organism.

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Abbreviations

Dg :

Desulfovibrio gigas

Dv :

Desulfovibrio vulgaris

SOD:

Superoxide dismutase

SOR:

Superoxide reductase

Tp :

Treponema pallidum

Tris:

Tris(hydroxymethyl)aminomethane

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Acknowledgements

This work was supported by the Fundação para a Ciência e Tecnologia (grants SFRH/BPD/12003/2003 and SFRH/BDP/14067/2003).

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Correspondence to José J. G. Moura.

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Auchère, F., Pauleta, S.R., Tavares, P. et al. Kinetics studies of the superoxide-mediated electron transfer reactions between rubredoxin-type proteins and superoxide reductases. J Biol Inorg Chem 11, 433–444 (2006). https://doi.org/10.1007/s00775-006-0090-0

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