Direct recordings of electron currents mediated by cytochromes b561 (CYB561) are not available yet, despite the importance of these proteins in a variety of physiological functions, including neurotransmitter synthesis and dietary iron uptake. Here, we used the two-electrode voltage-clamp technique applied to Xenopus oocytes to demonstrate, for the first time, the generation of electron currents by a Drosophila member of the CYB561 superfamily named stromal cell-derived receptor 2 (SDR2). This experimental method, along with the theoretical development of a three-state kinetic model, supports the hypothesis that electron donor/acceptor concentrations and transmembrane voltage mutually control SDR2-mediated electron transport activity in a complex but predictable manner. Antioxid. Redox Signal. 21, 384-391. © Mary Ann Liebert, Inc.

How are cytochrome b561 electron currents controlled by membrane voltage and substrate availability?

Trost, Paolo;Carpaneto, Armando
2014-01-01

Abstract

Direct recordings of electron currents mediated by cytochromes b561 (CYB561) are not available yet, despite the importance of these proteins in a variety of physiological functions, including neurotransmitter synthesis and dietary iron uptake. Here, we used the two-electrode voltage-clamp technique applied to Xenopus oocytes to demonstrate, for the first time, the generation of electron currents by a Drosophila member of the CYB561 superfamily named stromal cell-derived receptor 2 (SDR2). This experimental method, along with the theoretical development of a three-state kinetic model, supports the hypothesis that electron donor/acceptor concentrations and transmembrane voltage mutually control SDR2-mediated electron transport activity in a complex but predictable manner. Antioxid. Redox Signal. 21, 384-391. © Mary Ann Liebert, Inc.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11567/929774
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