(Q42146275)

English

Energy-linked nicotinamide nucleotide transhydrogenase 1963-1988: a commentary on 'Equilibrium Studies of the Energy-Dependent and Non-Energy-Dependent Pyridine Nucleotide Transhydrogenase Reactions'.

scientific article published on January 1989

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3 October 2019

Energy-linked nicotinamide nucleotide transhydrogenase 1963-1988: a commentary on 'Equilibrium Studies of the Energy-Dependent and Non-Energy-Dependent Pyridine Nucleotide Transhydrogenase Reactions' (English)

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3 October 2019

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C P Lee

1

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3 October 2019

L Ernster

2

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3 October 2019

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1 January 1989

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3 October 2019

Biochimica et Biophysica Acta

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3 October 2019

1000

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3 October 2019

371-376

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3 October 2019

Demonstration of a mitochondrial energy-dependent pyridine nucleotide transhydrogenase reaction

1 reference

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EVIDENCE FOR ENERGY-COUPLING IN NON-PHOSPHORYLATING ELECTRON TRANSPORT PARTICLES FROM BEEF-HEART MITOCHONDRIA

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Studies of the energy-transfer system of submitochondrial particles. I. Competition between oxidative phosphorylation and the energy-linked nicotinamide-adenine dinucleotide transhydrogenase reaction

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BIOLOGICAL OXIDOREDUCTIONS.

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Physiological roles of nicotinamide nucleotide transhydrogenase

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Stereochemistry of hydrogen-transfer in the energy-linked pyridine nucleotide transhydrogenase and related reactions

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Steady-state kinetics of mitochondrial nicotinamide nucleotide transhydrogenase. 1. The nonenergy-linked reaction.

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Steady-state kinetics of mitochondrial nicotinamide nucleotide transhydrogenase. 2. The energy-linked reaction

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Factors governing the kinetics and steady state of the mitochondrial nicotinamide nucleotide transhydrogenase system.

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Affinity chromatography of mitochondrial nicotinamide nucleotide transhydrogenase

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Nucleotide sequence of the pntA and pntB genes encoding the pyridine nucleotide transhydrogenase of Escherichia coli.

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Purification and molecular properties of reconstitutively active nicotinamide nucleotide transhydrogenase from beef heart mitochondria

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Purification and partial characterization of bovine heart mitochondrial pyridine dinucleotide transhydrogenase

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The subunit structure of bovine heart mitochondrial transhydrogenase

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Interaction of purified nicotinamidenucleotide transhydrogenase with dicyclohexylcarbodiimide

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Effects of N,N'-dicyclohexylcarbodiimide and N-(ethoxycarbonyl)-2-ethoxy-1,2-dihydroquinoline on hydride ion transfer and proton translocation activities of mitochondrial nicotinamidenucleotide transhydrogenase

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7 January 2021

Mitochondrial nicotinamide nucleotide transhydrogenase: active site modification by 5'-[p-(fluorosulfonyl)benzoyl]adenosine

1 reference

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7 January 2021

Energy-linked nicotinamide nucleotide transhydrogenase: hydrodynamic properties and active form of purified and membrane-bound mitochondrial transhydrogenase from beef heart

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7 January 2021

On the presence of a nicotinamide nucleotide transhydrogenase in mitochondria from potato tuber

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Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism

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Mechanism of phosphorylation in the respiratory chain

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Evidence discriminating between the Chemical and the Chemiosmotic Mechanisms of Electron Transport Phosphorylation

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Electric fields in coupling membranes

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Possible functions of chains of catalysts

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Studies of the energy-transfer system of submitochondrial particles. Kinetic studies of the effect of oligomycin on the respiratory chain of EDTA particles.

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7 January 2021

Chemical and Chemiosmotic Aspects of Electron Transport-Linked Phosphorylation

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A minimal hypothesis for membrane-linked free-energy transduction. The role of independent, small coupling units

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Uncoupler-inhibitor titrations of ATP-driven reverse electron transfer in bovine submitochondrial particles provide evidence for direct interaction between ATPase and NADH:Q oxidoreductase

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7 January 2021

Mechanisms of energy conservation in the mitochondrial membrane

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Studies of the Energy-Transfer System of Submitochondrial Particles. Fluorochrome Response as a Measure of the Energized State

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7 January 2021

ATP-driven transhydrogenase provides an example of delocalized chemiosmotic coupling in reconstituted vesicles and in submitochondrial particles

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The nicotinamide nucleotide specificity of glutamate dehydrogenase in intact rat-liver mitochondria.

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Hydroperoxide metabolism in mammalian organs

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Oxidative stress studied in intact mammalian cells

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Catecholamine control of enzymes involved in isocitrate oxidation of rat liver mitochondria

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Role of calcium in the hormonal regulation of liver metabolism

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Thyroid hormone action on mitochondria. IV. Redox states of intrinsic pyridine nucleotides in hypothyroidism, and influence of L-thyroxine

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The efficiency of oxidative phosphorylation and the rapid control by thyroid hormone of nicotinamide nucleotide reduction and transhydrogenation in intact rat liver mitochondria

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Comparative studies on nicotinamide nucleotide transhydrogenase from different sources

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10.1016/S0006-3002(89)80032-0

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PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:2673389%20AND%20SRC:MED&resulttype=core&format=json

3 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:2673389%20AND%20SRC:MED&resulttype=core&format=json

3 October 2019

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