Zobrazeno 1 - 10
of 166
pro vyhledávání: '"Alexei A. Stuchebrukhov"'
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-12 (2023)
Abstract In all resolved structures of complex I, there exists a tunnel-like Q-chamber for ubiquinone binding and reduction. The entrance to the Q-chamber in ND1 subunit forms a narrow bottleneck, which is rather tight and requires thermal conformati
Externí odkaz:
https://doaj.org/article/9ab9f4779eca45a1a257131a568aea5e
Autor:
Yang Ni, Muhammad A. Hagras, Vassiliki Konstantopoulou, Johannes A. Mayr, Alexei A. Stuchebrukhov, David Meierhofer
Publikováno v:
Cells, Vol 8, Iss 10, p 1149 (2019)
Complex I (CI) is the first enzyme of the mitochondrial respiratory chain and couples the electron transfer with proton pumping. Mutations in genes encoding CI subunits can frequently cause inborn metabolic errors. We applied proteome and metabolome
Externí odkaz:
https://doaj.org/article/3ebb9eafc0df45e6a10e070e144eec65
Publikováno v:
The journal of physical chemistry. B, vol 127, iss 19
Autoxidation of tartaric acid in air-saturated aqueous solutions in the presence of Fe(II) at low pH, 2.5, shows autocatalytic behavior with distinct initiation, propagation, and termination phases. With increasing pH, the initiation phase speeds up,
Publikováno v:
FEBS Letters. 597:237-245
Complex I is a key proton-pumping enzyme in bacterial and mitochondrial respiratory electron transport chains. Using quantum chemistry and electrostatic calculations, we have examined the pKa of the reduced quinone QH-/QH2 in the catalytic cavity of
Publikováno v:
Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology, vol 21, iss 1
Photochemical & Photobiological Sciences
Photochemical & Photobiological Sciences
At the joint between the membrane and hydrophilic arms of the enzyme, the structure of the respiratory complex I reveals a tunnel-like Q-chamber for ubiquinone binding and reduction. The narrow entrance of the quinone chamber located in ND1 subunit f
Publikováno v:
The journal of physical chemistry. B. 126(32)
Proton migration on biological membranes plays a major role in cellular respiration and photosynthesis, but it is not yet fully understood. Here we show that proton dissociation kinetics and related geminate recombination can be used as a probe of su
Publikováno v:
Biophysical Journal. 122:136a
We apply linear response theory to calculate mechanical allosteric couplings in respiratory complex I between the iron sulfur cluster N2, located in the catalytic cavity, and the membrane part of the enzyme, separated from it by more than 50 Å. Acco
Publikováno v:
The Journal of Physical Chemistry B. 123:5265-5273
Respiratory complex I catalyzes two-electron/two-proton reduction of a ubiquinone (Q) substrate bound at its Q-binding pocket; upon reduction, ubiquinole carries electrons further down the electron transport chain. The mechanism of this two-electron
Publikováno v:
Biochimica et biophysica acta. Bioenergetics. 1861(7)
Components of respiratory chains in mitochondria and some aerobic bacteria assemble into larger, multiprotein membrane-bound supercomplexes. Here, we address the functional significance of supercomplexes composed of respiratory-chain complexes III an
Autor:
Alexei A. Stuchebrukhov
Publikováno v:
The journal of physical chemistry. B. 123(44)
Complexes I to IV, with the exception of Complex II, are redox-driven proton pumps that convert redox energy of oxygen reduction to proton gradient across the mitochondrial or bacterial membrane; in turn, the created electrochemical gradient drives t