Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I

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Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/BI7009822
P932PMC publication ID2258335
P698PubMed publication ID17760425
P5875ResearchGate publication ID6080729

P50authorAlexander KotlyarQ51658307
Vera GrivennikovaQ61820726
P2093author name stringJoel S Karliner
Gary Cecchini
Andrei D Vinogradov
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Mitochondrial NADH-ubiquinone oxidoreductase (Complex I). Effect of substrates on the fragmentation of subunits by trypsinQ46171503
Conformation-driven and semiquinone-gated proton-pump mechanism in the NADH-ubiquinone oxidoreductase (complex I).Q46648740
A novel strong competitive inhibitor of complex I.Q46656137
Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chainQ47729468
The flavoprotein subcomplex of complex I (NADH:ubiquinone oxidoreductase) from bovine heart mitochondria: insights into the mechanisms of NADH oxidation and NAD+ reduction from protein film voltammetry.Q51921590
Steady-state kinetics of the reduction of coenzyme Q analogs by complex I (NADH:ubiquinone oxidoreductase) in bovine heart mitochondria and submitochondrial particles.Q52310261
The effect of delta mu H+ on the interaction of rotenone with complex I of submitochondrial particles.Q52442645
Slow active/inactive transition of the mitochondrial NADH-ubiquinone reductase.Q52449151
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Interaction of the mitochondrial NADH-ubiquinone reductase with rotenone as related to the enzyme active/inactive transition.Q52552962
-->H+/2e- stoichiometry in NADH-quinone reductase reactions catalyzed by bovine heart submitochondrial particles.Q52570957
The complex I from Rhodobacter capsulatus.Q54134715
ATR-FTIR Redox Difference Spectroscopy ofYarrowia lipolyticaand Bovine Complex I†Q58782224
The Redox-Bohr Group Associated with Iron-Sulfur Cluster N2 of Complex IQ58782339
Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redox-gated ligand conductionQ58782802
New evidence for the dimeric nature of NADH:Q oxidoreductase in bovine-heart submitochondrial particlesQ67295594
Tight-binding inhibitors-I. Kinetic behaviorQ67364914
Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinoneQ70201544
Reductive inactivation of the mitochondrial three subunit NADH dehydrogenaseQ70462648
Interaction of the membrane-bound succinate dehydrogenase with substrate and competitive inhibitorsQ71255402
Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (complex I) and the pseudo-reversible active/inactive enzyme transitionQ74567714
Studies on the respiratory chain-linked dihydrodiphosphopyridine nucleotide dehydrogenase. I. Assay of the enzyme in particulate and in soluble preparationsQ79020294
P433issue38
P407language of work or nameEnglishQ1860
P304page(s)10971-10978
P577publication date2007-08-31
P1433published inBiochemistryQ764876
P1476titleRedox-dependent change of nucleotide affinity to the active site of the mammalian complex I
P478volume46

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cites work (P2860)
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Q48018687Warm preconditioning protects against acute heat-induced respiratory dysfunction and delays bleaching in a symbiotic sea anemone.
Q41393384What are the sources of hydrogen peroxide production by heart mitochondria?

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