Kinetic characteristics of the proton-pumping NADH: quinone reductases (respiratory
complexes I) are reviewed. Unsolved problems of the redox-linked proton translocation …

The aerobic respiratory chain of Escherichia coli contains several primary dehydrogenases,
including NADH dehydrogenase, succinate dehydrogenase, and D-lactate dehydrogenase …

Escherichia coli is known to couple aerobic respiratory catabolism to ATP synthesis by virtue
of the primary generators of the proton motive force—NADH dehydrogenase I, cytochrome …

Bacterial polysulfide reductase (PsrABC) is an integral membrane protein complex
responsible for quinone-coupled reduction of polysulfide, a process important in extreme …

Tightly coupled bovine heart submitochondrial particles treated to activate complex I and to
block ubiquinol oxidation were capable of rapid uncoupler-sensitive inside-directed proton …

The proton-pumping NADH: ubiquinone oxidoreductase, also called complex I, is the entry
point for electrons into the respiratory chains of many bacteria and mitochondria of most …

Complex I of respiratory chains is an energy transducing enzyme present in most bacteria,
mitochondria and chloroplasts. It catalyzes the oxidation of NADH and the reduction of …

Respiratory complex I couples electron transfer between NADH and ubiquinone to proton
translocation across an energy-transducing membrane to support the proton-motive force …

Complex I (NADH: ubiquinone oxidoreductase) plays a central role in cellular energy
production, coupling electron transfer between NADH and quinone to proton translocation. It …

Complex I (NADH-ubiquinone oxidoreductase) in the respiratory chain of mitochondria and
several bacteria functions as a redox-driven proton pump that contributes to the generation …