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http://purl.uniprot.org/citations/10924914http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10924914http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10924914http://www.w3.org/2000/01/rdf-schema#comment"Mitochondrial proton-translocating NADH-dehydrogenase (complex I) is one of the largest and most complicated membrane bound protein complexes. Despite its central role in eukaryotic oxidative phosphorylation and its involvement in a broad range of human disorders, little is known about its structure and function. Therefore, we have started to use the powerful genetic tools available for the strictly aerobic yeast Yarrowia lipolytica to study this respiratory chain enzyme. To establish Y. lipolytica as a model system for complex I, we purified and characterized the multisubunit enzyme from Y lipolytica and sequenced the nuclear genes coding for the seven central subunits of its peripheral part. Complex I from Y lipolytica is quite stable and could be isolated in a highly pure and monodisperse state. One binuclear and four tetranuclear iron-sulfur clusters, including N5, which was previously known only from mammalian mitochondria, were detected by EPR spectroscopy. Initial structural analysis by single particle electron microscopy in negative stain and ice shows complex I from Y. lipolytica as an L-shaped particle that does not exhibit a thin stalk between the peripheral and the membrane parts that has been observed in other systems."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.org/dc/terms/identifier"doi:10.1016/S0005-2728(00)00154-7"xsd:string
http://purl.uniprot.org/citations/10924914http://purl.org/dc/terms/identifier"doi:10.1016/s0005-2728(00)00154-7"xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Brandt U."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Brandt U."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Schaegger H."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Schagger H."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Zwicker K."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Zwicker K."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Kerscher S."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Kerscher S."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Lindahl M."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Lindahl M."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Radermacher M."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Radermacher M."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Djafarzadeh Andabili R."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/author"Djafarzadeh R."xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/name"Biochim. Biophys. Acta"xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/name"Biochim Biophys Acta"xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/pages"230-238"xsd:string
http://purl.uniprot.org/citations/10924914http://purl.uniprot.org/core/pages"230-238"xsd:string