TY  - JOUR
A1  - Galkin, Alexander
A1  - Meyer, Björn
A1  - Wittig, Ilka
A1  - Karas, Michael
A1  - Schägger, Hermann
A1  - Vinogradov, Andrei
A1  - Brandt, Ulrich
T1  - Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I
T2  - Journal of biological chemistry
N2  - Mitochondrial complex I (NADH:ubiquinone oxidoreductase) undergoes reversible deactivation upon incubation at 30–37 °C. The active/deactive transition could play an important role in the regulation of complex I activity. It has been suggested recently that complex I may become modified by S-nitrosation under pathological conditions during hypoxia or when the nitric oxide:oxygen ratio increases. Apparently, a specific cysteine becomes accessible to chemical modification only in the deactive form of the enzyme. By selective fluorescence labeling and proteomic analysis, we have identified this residue as cysteine-39 of the mitochondrially encoded ND3 subunit of bovine heart mitochondria. Cysteine-39 is located in a loop connecting the first and second transmembrane helix of this highly hydrophobic subunit. We propose that this loop connects the ND3 subunit of the membrane arm with the PSST subunit of the peripheral arm of complex I, placing it in a region that is known to be critical for the catalytic mechanism of complex I. In fact, mutations in three positions of the loop were previously reported to cause Leigh syndrome with and without dystonia or progressive mitochondrial disease.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76347
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-763476
SN  - 0021-9258
VL  - 283
IS  - 30
SP  - 20907
EP  - 20913
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -