Steady-state kinetics of the reduction of coenzyme Q analogs by complex I (NADH:ubiquinone oxidoreductase) in bovine heart mitochondria and submitochondrial particles.
about
Redox-dependent change of nucleotide affinity to the active site of the mammalian complex IIschemic A/D transition of mitochondrial complex I and its role in ROS generationModeling of mitochondria bioenergetics using a composable chemiosmotic energy transduction rate law: theory and experimental validationA critical appraisal of the mitochondrial coenzyme Q pool.Kinetics and regulation of mammalian NADH-ubiquinone oxidoreductase (Complex I).Genetic evidence for NAD(P)H:quinone oxidoreductase 1-catalyzed quinone reduction on passage through the mouse pulmonary circulation.Isoflurane selectively inhibits distal mitochondrial complex I in Caenorhabditis elegansMitochondrial production of oxygen radical species and the role of Coenzyme Q as an antioxidant.Coenzyme Q(1) as a probe for mitochondrial complex I activity in the intact perfused hyperoxia-exposed wild-type and Nqo1-null mouse lung.Genome Analysis of Structure-Function Relationships in Respiratory Complex I, an Ancient Bioenergetic EnzymeModeling mitochondrial function.Kinetics of integrated electron transfer in the mitochondrial respiratory chain: random collisions vs. solid state electron channeling.Coenzyme Q1 redox metabolism during passage through the rat pulmonary circulation and the effect of hyperoxiaNew developments on the functions of coenzyme Q in mitochondria.Characterisation of the active/de-active transition of mitochondrial complex I.NADH oxidation by the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae: functional role of the NqrF subunit.Probing the ubiquinone reduction site of mitochondrial complex I using novel cationic inhibitors.Role of mitochondrial complex I and protective effect of CoQ10 supplementation in propofol induced cytotoxicity.Purification of Ovine Respiratory Complex I Results in a Highly Active and Stable Preparation.Investigation of the mechanism of proton translocation by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria: does the enzyme operate by a Q-cycle mechanism?The METTL20 Homologue from Agrobacterium tumefaciens Is a Dual Specificity Protein-lysine Methyltransferase That Targets Ribosomal Protein L7/L12 and the β Subunit of Electron Transfer Flavoprotein (ETFβ).Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (Complex I) and production of reactive oxygen species.Differential effects of mitochondrial Complex I inhibitors on production of reactive oxygen species.Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex I.The mitochondrial respiratory chain is partially organized in a supercomplex assembly: kinetic evidence using flux control analysis.The higher plant plastid NAD(P)H dehydrogenase-like complex (NDH) is a high efficiency proton pump that increases ATP production by cyclic electron flow.Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I.Decrease of rotenone inhibition is a sensitive parameter of complex I damage in brain non-synaptic mitochondria of aged rats.The Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio alginolyticus--redox states of the FAD prosthetic group and mechanism of Ag+ inhibition.Role of mitochondrial electron transport complex I in coenzyme Q1 reduction by intact pulmonary arterial endothelial cells and the effect of hyperoxia.Three classes of inhibitors share a common binding domain in mitochondrial complex I (NADH:ubiquinone oxidoreductase).Probing substrate binding site of the Escherichia coli quinol oxidases using synthetic ubiquinol analogues.A high diffusion coefficient for coenzyme Q10 might be related to a folded structure
P2860
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P2860
Steady-state kinetics of the reduction of coenzyme Q analogs by complex I (NADH:ubiquinone oxidoreductase) in bovine heart mitochondria and submitochondrial particles.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh-hant
name
Steady-state kinetics of the r ...... nd submitochondrial particles.
@en
Steady-state kinetics of the reduction of coenzyme Q analogs by complex I
@nl
type
label
Steady-state kinetics of the r ...... nd submitochondrial particles.
@en
Steady-state kinetics of the reduction of coenzyme Q analogs by complex I
@nl
prefLabel
Steady-state kinetics of the r ...... nd submitochondrial particles.
@en
Steady-state kinetics of the reduction of coenzyme Q analogs by complex I
@nl
P2093
P356
P1433
P1476
Steady-state kinetics of the r ...... nd submitochondrial particles.
@en
P2093
Di Bernardo S
Estornell E
Pallotti F
Parenti Castelli G
P304
P356
10.1021/BI9516034
P407
P577
1996-02-01T00:00:00Z