Erv1 and Cytochrome c Mediate Rapid Electron Transfer via A Collision-Type Interaction |
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Affiliation: | 1. Institute for Biochemistry, Redox Biochemistry, University of Cologne, Zuelpicher Str. 47a, 50674 Cologne, Germany;2. VIB-VUB Center for Structural Biology, Pleinlaan 2, 1050 Brussels, Belgium;3. Jean Jeener NMR Centre, VUB, Pleinlaan 2, 1050 Brussels, Belgium;4. Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, 50931Cologne, Germany |
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Abstract: | Being essential for oxidative protein folding in the mitochondrial intermembrane space, the mitochondrial disulfide relay relies on the electron transfer (ET) from the sulfhydryl oxidase Erv1 to cytochrome c (Cc). Using solution NMR spectroscopy, we demonstrate that while the yeast Cc-Erv1 system is functionally active, no observable binding of the protein partners takes place. The transient interaction between Erv1 and Cc can be rationalized by molecular modeling, suggesting that a large surface area of Erv1 can sustain a fast ET to Cc via a collision-type mechanism, without the need for a canonical protein complex formation. We suggest that, by preventing the direct ET to molecular oxygen (O2), the collision-type Cc-Erv1 interaction plays a role in protecting the organism against reactive oxygen species. |
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Keywords: | Erv1 electron transfer transient protein complex disulfide relay |
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