Thorsten Friedrich focuses on Biochemistry, Oxidoreductase, NADH dehydrogenase, Respiratory chain and Stereochemistry. His is doing research in Protein subunit, Neurospora crassa, Escherichia coli, Mitochondrion and Purple bacteria, both of which are found in Biochemistry. His Escherichia coli research is multidisciplinary, incorporating perspectives in Membrane, Polyethylene glycol and Titration.
The study incorporates disciplines such as Electron transport chain, Biophysics, Chemiosmosis, Electron transfer and Piericidin A in addition to Oxidoreductase. He focuses mostly in the field of Respiratory chain, narrowing it down to matters related to Proton transport and, in some cases, Oxoglutarate dehydrogenase complex, NADH dehydrogenase complex and Cytochrome c oxidase. Thorsten Friedrich frequently studies issues relating to Redox and Stereochemistry.
Thorsten Friedrich mainly focuses on Biochemistry, Oxidoreductase, Escherichia coli, Stereochemistry and Electron transfer. His research related to Enzyme, Cofactor, Cytochrome, Respiratory chain and Mutant might be considered part of Biochemistry. The various areas that Thorsten Friedrich examines in his Oxidoreductase study include NADH dehydrogenase, Protein subunit, Membrane, Flavin mononucleotide and Redox.
His Escherichia coli research includes themes of Cytoplasm, Biogenesis, Iron–sulfur cluster and Microbiology. His Stereochemistry research focuses on Electron Transport Complex I and how it relates to Protein structure. He works mostly in the field of Electron transfer, limiting it down to concerns involving Electron transport chain and, occasionally, Chemiosmosis.
Thorsten Friedrich mainly investigates Biochemistry, Escherichia coli, Cytochrome, Oxidoreductase and Electron transfer. His Biochemistry study focuses mostly on Cofactor, Enzyme, Oxidative phosphorylation, Protein subunit and Reductase. His research investigates the connection between Escherichia coli and topics such as Microbiology that intersect with problems in Bacterial Model.
His Oxidoreductase research incorporates elements of Chemical physics, Aquifex aeolicus, Cytoplasm, Cysteine and Stereochemistry. His Electron transfer research incorporates themes from Electron transport chain, Electron Transport Complex I, Membrane, Redox and Quinone. His research investigates the link between Iron–sulfur cluster and topics such as NADH dehydrogenase that cross with problems in Piericidin A.
His primary areas of investigation include Biochemistry, Oxidoreductase, Electron transfer, Electron transport chain and Cytochrome. His Oxidoreductase study combines topics from a wide range of disciplines, such as Stereochemistry and Escherichia coli. His work is dedicated to discovering how Escherichia coli, Cytoplasm are connected with Mitochondrion, Fluorescence recovery after photobleaching, Respiratory chain, Polyacrylamide gel electrophoresis and Mutant and other disciplines.
His study in Electron transfer is interdisciplinary in nature, drawing from both Membrane and Redox. While the research belongs to areas of Electron transport chain, Thorsten Friedrich spends his time largely on the problem of Electron Transport Complex I, intersecting his research to questions surrounding Flavin mononucleotide and Iron–sulfur cluster. The Cytochrome study combines topics in areas such as Oxidase test, Cytochrome c oxidase and Heme.
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The respiratory-chain NADH dehydrogenase (complex I) of mitochondria
Hanns Weiss;Thorsten Friedrich;Götz Hofhaus;Dagmar Preis.
FEBS Journal (1991)
The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.
Thorsten Friedrich;Dierk Scheide.
FEBS Letters (2000)
The Gene Locus of the Proton-translocating NADH : Ubiquinone Oxidoreductase in Escherichia coli: Organization of the 14 Genes and Relationship Between the Derived Proteins and Subunits of Mitochondrial Complex I
Uwe Weidner;Stephan Geier;Arne Ptock;Thorsten Friedrich.
Journal of Molecular Biology (1993)
Isolation and Characterization of the Proton-translocating NADH:ubiquinone Oxidoreductase from Escherichia coli
Hans Leif;Vladimir D. Sled;Vladimir D. Sled;Tomoko Ohnishi;Hanns Weiss.
FEBS Journal (1995)
The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts
Thorsten Friedrich;Klaus Steinmüller;Hanns Weiss.
FEBS Letters (1995)
Two binding sites of inhibitors in NADH: ubiquinone oxidoreductase (complex I). Relationship of one site with the ubiquinone-binding site of bacterial glucose:ubiquinone oxidoreductase.
Thorsten Friedrich;Petra Van Heek;Hans Leif;Tomoko Ohnishi.
FEBS Journal (1994)
Consistent structure between bacterial and mitochondrial NADH:Ubiquinone oxidoreductase (Complex I)
Vincent Guénebaut;Angela Schlitt;Hanns Weiss;Kevin Leonard.
Journal of Molecular Biology (1998)
Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules.
Thorsten Friedrich;Hanns Weiss.
Journal of Theoretical Biology (1997)
An anaerobic mitochondrion that produces hydrogen
Brigitte Boxma;Rob M. de Graaf;Georg W.M. van der Staay;Theo A. van Alen.
Nature (2005)
THE NADH:UBIQUINONE OXIDOREDUCTASE (COMPLEX I) FROM ESCHERICHIA COLI
Thorsten Friedrich.
Biochimica et Biophysica Acta (1998)
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