Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 433, Issue 15, Pages -Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2021.167045
Keywords
Erv1; cytochrome c; electron transfer; transient protein complex; disulfide relay
Categories
Funding
- Deutsche Forschungsgemeinschaft (DFG) [251546152, 435235019, 269925409, 411422114]
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In the mitochondrial intermembrane space, the yeast cytochrome c-Erv1 system achieves rapid electron transfer through a collision-type mechanism without the need for protein complex formation. This interaction helps prevent direct electron transfer to molecular oxygen, protecting the organism against reactive oxygen species.
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 (O-2), the collision-type Cc-Erv1 interaction plays a role in protecting the organism against reactive oxygen species. (C) 2021 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
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