Grivennikova, Vera G Gladyshev, Grigory V Vinogradov, Andrei D
Published in
Biochimica et biophysica acta. Bioenergetics
Mitochondrial NADH:ubiquinone oxidoreductase (proton translocating respiratory complex I) serves several essential functions in cell metabolism: it maintains the intramitochondrial NADH/NAD+ ratio, contributes to generation of the proton-motive force, and participates in physiological and/or pathophysiological production of so-called reactive oxyge...
Wright, John J. Fedor, Justin G. Hirst, Judy Roessler, Maxie M.
Published in
BMC Biology
BackgroundFor decades, semiquinone intermediates have been suggested to play an essential role in catalysis by one of the most enigmatic proton-pumping enzymes, respiratory complex I, and different mechanisms have been proposed on their basis. However, the difficulty in investigating complex I semiquinones, due to the many different enzymes embedde...
Wright, JJ Fedor, J Hirst, J Roessler, M
Background. For decades semiquinone intermediates have been suggested to play an essential role in catalysis by one of the most enigmatic proton-pumping enzymes, respiratory complex I, and different mechanisms have been proposed on their basis. However, the difficulty in investigating complex I semiquinones, due to the many different enzymes embedd...
Skorupa, Philipp Lindenstrauß, Ute Burschel, Sabrina Blumenscheit, Christian Friedrich, Thorsten Pinske, Constanze
Published in
FEBS open bio
Formate hydrogenlyase (FHL) is the main hydrogen-producing enzyme complex in enterobacteria. It converts formate to CO2 and H2 via a formate dehydrogenase and a [NiFe]-hydrogenase. FHL and complex I are evolutionarily related and share a common core architecture. However, complex I catalyses the fundamentally different electron transfer from NADH t...
Wright, John J. Fedor, Justin G. Hirst, Judy Roessler, Maxie M.
Abstract: Background: For decades, semiquinone intermediates have been suggested to play an essential role in catalysis by one of the most enigmatic proton-pumping enzymes, respiratory complex I, and different mechanisms have been proposed on their basis. However, the difficulty in investigating complex I semiquinones, due to the many different enz...
Chen, Qun Thompson, Jeremy Hu, Ying Dean, Joseph Lesnefsky, Edward J
Published in
American journal of physiology. Cell physiology
Activation of calpain 1 (CPN1) and calpain 2 (CPN2) contributes to cardiac injury during ischemia (ISC) and reperfusion (REP). Complex I activity is decreased in heart mitochondria following ISC-REP. CPN1 and CPN2 are ubiquitous calpains that exist in both cytosol (cs)-CPN1 and 2 and mitochondria (mit)-CPN1 and 2. Recent work shows that the complex...
Agip, Noor Blaza, James N Fedor, Justin Hirst, Judy
Single-particle electron cryomicroscopy (cryo-EM) has led to a revolution in structural work on mammalian respiratory complex I. Complex I (mitochondrial NADH:ubiquinone oxidoreductase), a membrane-bound redox-driven proton pump, is one of the largest and most complicated enzymes in the mammalian cell. Rapid progress, following the first 5-Å resolu...
Agip, Ahmed-Noor A. Blaza, James N. Fedor, Justin G. Hirst, Judy
Published in
Annual Review of Biophysics
Single-particle electron cryomicroscopy (cryo-EM) has led to a revolution in structural work on mammalian respiratory complex I. Complex I (mitochondrial NADH:ubiquinone oxidoreductase), a membrane-bound redox-driven proton pump, is one of the largest and most complicated enzymes in the mammalian cell. Rapid progress, following the first 5-Å resolu...
Di Luca, Andrea Mühlbauer, Max E Saura, Patricia Kaila, Ville R I
Published in
Biochimica et biophysica acta. Bioenergetics
The respiratory complex I is a redox-driven proton pump that employs the free energy released from quinone reduction to pump protons across its complete ca. 200 Å wide membrane domain. Despite recently resolved structures and molecular simulations, the exact mechanism for the proton transport process remains unclear. Here we combine large-scale mol...
Maclean, Andrew E Hertle, Alexander P Ligas, Joanna Bock, Ralph Balk, Janneke Meyer, Etienne H
Published in
Current biology : CB
Parasitism is a life history strategy found across all domains of life whereby nutrition is obtained from a host. It is often associated with reductive evolution of the genome, including loss of genes from the organellar genomes [1, 2]. In some unicellular parasites, the mitochondrial genome (mitogenome) has been lost entirely, with far-reaching co...