Year: 2021
Type: article
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.
Source: Journal of Molecular Biology
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,310
Awards: Redoxregulation der menschlichen Adenylatkinase 2 (AK2), einem essentiellen Schlüsselenzym des zellulären Energiemetabolismus, G1179449648, G1298078298, G1506585195, G1966564134, G2253231869, GRK 2550: Dynamische Regulation zellulärer Proteinlokalisationen, G451293389, G5542483417, G563450409, SFB 1218: Regulation der zellulären Funktion durch Mitochondrien, Neue Interaktionspartner der Sulfhydryl : Cytochrom c Oxidoreduktase ALR
OpenAlex ID: W3163131075