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The redox driven Na+-pumping mechanism in Vibrio cholerae NADH-quinone oxidoreductase relies on dynamic conformational changes
by
Masuya, Takahiro
, Ishikawa-Fukuda, Moe
, Barquera, Blanca
, Kato, Takayuki
, Okazaki, Kei-ichi
, Murai, Masatoshi
, Seki, Takehito
, Kishikawa, Jun-ichi
, Miyoshi, Hideto
in
101/28
/ 119/118
/ 631/45/173
/ 631/535/1258/1259
/ 631/57/2272/2273
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Cofactors
/ Cryoelectron Microscopy
/ Electron microscopy
/ Electron transfer
/ Electron Transport
/ Electrons
/ Enzymes
/ Humanities and Social Sciences
/ Molecular dynamics
/ Molecular Dynamics Simulation
/ multidisciplinary
/ Na+/K+-exchanging ATPase
/ NADH
/ NADH-quinone oxidoreductase
/ Nicotinamide adenine dinucleotide
/ Oxidation-Reduction
/ Protein Conformation
/ Pumping
/ Quinone oxidoreductase
/ Quinone Reductases - chemistry
/ Quinone Reductases - genetics
/ Quinone Reductases - metabolism
/ Quinones
/ Science
/ Science (multidisciplinary)
/ Sodium
/ Sodium - metabolism
/ Translocation
/ Vibrio cholerae
/ Vibrio cholerae - enzymology
/ Vibrio cholerae - genetics
/ Vibrio cholerae - metabolism
2026
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The redox driven Na+-pumping mechanism in Vibrio cholerae NADH-quinone oxidoreductase relies on dynamic conformational changes
by
Masuya, Takahiro
, Ishikawa-Fukuda, Moe
, Barquera, Blanca
, Kato, Takayuki
, Okazaki, Kei-ichi
, Murai, Masatoshi
, Seki, Takehito
, Kishikawa, Jun-ichi
, Miyoshi, Hideto
in
101/28
/ 119/118
/ 631/45/173
/ 631/535/1258/1259
/ 631/57/2272/2273
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Cofactors
/ Cryoelectron Microscopy
/ Electron microscopy
/ Electron transfer
/ Electron Transport
/ Electrons
/ Enzymes
/ Humanities and Social Sciences
/ Molecular dynamics
/ Molecular Dynamics Simulation
/ multidisciplinary
/ Na+/K+-exchanging ATPase
/ NADH
/ NADH-quinone oxidoreductase
/ Nicotinamide adenine dinucleotide
/ Oxidation-Reduction
/ Protein Conformation
/ Pumping
/ Quinone oxidoreductase
/ Quinone Reductases - chemistry
/ Quinone Reductases - genetics
/ Quinone Reductases - metabolism
/ Quinones
/ Science
/ Science (multidisciplinary)
/ Sodium
/ Sodium - metabolism
/ Translocation
/ Vibrio cholerae
/ Vibrio cholerae - enzymology
/ Vibrio cholerae - genetics
/ Vibrio cholerae - metabolism
2026
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The redox driven Na+-pumping mechanism in Vibrio cholerae NADH-quinone oxidoreductase relies on dynamic conformational changes
by
Masuya, Takahiro
, Ishikawa-Fukuda, Moe
, Barquera, Blanca
, Kato, Takayuki
, Okazaki, Kei-ichi
, Murai, Masatoshi
, Seki, Takehito
, Kishikawa, Jun-ichi
, Miyoshi, Hideto
in
101/28
/ 119/118
/ 631/45/173
/ 631/535/1258/1259
/ 631/57/2272/2273
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Cofactors
/ Cryoelectron Microscopy
/ Electron microscopy
/ Electron transfer
/ Electron Transport
/ Electrons
/ Enzymes
/ Humanities and Social Sciences
/ Molecular dynamics
/ Molecular Dynamics Simulation
/ multidisciplinary
/ Na+/K+-exchanging ATPase
/ NADH
/ NADH-quinone oxidoreductase
/ Nicotinamide adenine dinucleotide
/ Oxidation-Reduction
/ Protein Conformation
/ Pumping
/ Quinone oxidoreductase
/ Quinone Reductases - chemistry
/ Quinone Reductases - genetics
/ Quinone Reductases - metabolism
/ Quinones
/ Science
/ Science (multidisciplinary)
/ Sodium
/ Sodium - metabolism
/ Translocation
/ Vibrio cholerae
/ Vibrio cholerae - enzymology
/ Vibrio cholerae - genetics
/ Vibrio cholerae - metabolism
2026
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The redox driven Na+-pumping mechanism in Vibrio cholerae NADH-quinone oxidoreductase relies on dynamic conformational changes
Journal Article
The redox driven Na+-pumping mechanism in Vibrio cholerae NADH-quinone oxidoreductase relies on dynamic conformational changes
2026
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Overview
The Na
+
-pumping NADH-quinone oxidoreductase (Na
+
-NQR) is a key respiratory enzyme in many marine and pathogenic bacteria that couples electron transfer to Na
+
-pumping across the membrane. Earlier X-ray and cryo-electron microscopy structures of Na
+
-NQR from
Vibrio cholerae
suggested that the subunits harboring redox cofactors undergo conformational changes during catalytic turnover. However, these proposed rearrangements have not yet been confirmed. Here, we have identified at least five distinct conformational states of Na
+
-NQR using: mutants that lack specific cofactors, specific inhibitors or low-sodium conditions. Molecular dynamics simulations based on these structural insights indicate that 2Fe-2S reduction in NqrD/E plays a crucial role in triggering Na
+
translocation by driving structural rearrangements in the NqrD/E subunits, which subsequently influence NqrC and NqrF positioning. This study provides structural insights into the mechanism of Na
+
translocation coupled to electron transfer in Na⁺-NQR.
The Na
+
-pumping NADH-quinone oxidoreductase is a redox-driven sodium pump often found in pathogenic bacteria. Here, the authors demonstrate how enzyme structural changes efficiently couple electron transfer to Na
+
translocation.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 119/118
/ 82/83
/ Bacteria
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Enzymes
/ Humanities and Social Sciences
/ Molecular Dynamics Simulation
/ NADH
/ Nicotinamide adenine dinucleotide
/ Pumping
/ Quinone Reductases - chemistry
/ Quinone Reductases - genetics
/ Quinone Reductases - metabolism
/ Quinones
/ Science
/ Sodium
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