P185
The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondriaDirect assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonanceReversible interconversion of carbon dioxide and formate by an electroactive enzymeUnusual oxidative chemistry of N(omega)-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidaseAtomically defined mechanism for proton transfer to a buried redox centre in a proteinReplacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structureHigh-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparisonMechanisms of redox-coupled proton transfer in proteins: role of the proximal proline in reactions of the [3Fe-4S] cluster in Azotobacter vinelandii ferredoxin IModulation of heme redox potential in the cytochrome c6 familyEnergy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex IThe nuclear encoded subunits of complex I from bovine heart mitochondriaGRIM-19, a cell death regulatory gene product, is a subunit of bovine mitochondrial NADH:ubiquinone oxidoreductase (complex I)Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 2. Effects on heme coordination and function.The post-translational modifications of the nuclear encoded subunits of complex I from bovine heart mitochondria.The subunit composition of mitochondrial NADH:ubiquinone oxidoreductase (complex I) from Pichia pastoris.Exploring interactions between the 49 kDa and ND1 subunits in mitochondrial NADH-ubiquinone oxidoreductase (complex I) by photoaffinity labeling.Bovine complex I is a complex of 45 different subunits.Towards the molecular mechanism of respiratory complex I.Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I. Identification of two new subunits.The dichotomy of complex I: a sodium ion pump or a proton pump.Kinetic evidence against partitioning of the ubiquinone pool and the catalytic relevance of respiratory-chain supercomplexes.Interaction of the mitochondria-targeted antioxidant MitoQ with phospholipid bilayers and ubiquinone oxidoreductases.Production of reactive oxygen species by complex I (NADH:ubiquinone oxidoreductase) from Escherichia coli and comparison to the enzyme from mitochondria.The production of reactive oxygen species by complex I.Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymes.Reevaluating the relationship between EPR spectra and enzyme structure for the iron sulfur clusters in NADH:quinone oxidoreductaseMolecular features of biguanides required for targeting of mitochondrial respiratory complex I and activation of AMP-kinase.Structure of subcomplex Iβ of mammalian respiratory complex I leads to new supernumerary subunit assignmentsElucidating the mechanisms of coupled electron transfer and catalytic reactions by protein film voltammetry.A scalable, GFP-based pipeline for membrane protein overexpression screening and purification.A spectrophotometric coupled enzyme assay to measure the activity of succinate dehydrogenaseFormation and characterization of an all-ferrous Rieske cluster and stabilization of the [2Fe-2S]0 core by protonation.Investigating the function of [2Fe-2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potentialSubunit NDUFV3 is present in two distinct isoforms in mammalian complex I.Mitochondrial complex I.Oxidation-State-Dependent Binding Properties of the Active Site in a Mo-Containing Formate Dehydrogenase.The Enigma of the Respiratory Chain Supercomplex.Characterization of clinically identified mutations in NDUFV1, the flavin-binding subunit of respiratory complex I, using a yeast model system.The mechanism of catalysis by type-II NADH:quinone oxidoreductases.Mössbauer spectroscopy on respiratory complex I: the iron-sulfur cluster ensemble in the NADH-reduced enzyme is partially oxidized.
P50
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P50
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Physical Chemist
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Judy Hirst
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P166
P1053
F-4803-2011
P1153
7102628554
P184
P19
P2070
judy-hirst-13818
P21
P213
0000 0001 3579 1277
P31
P3829
P463
P4789
P496
0000-0001-8667-6797