Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Heike Angerer"'
Autor:
Etienne Galemou Yoga, Kristian Parey, Amina Djurabekova, Outi Haapanen, Karin Siegmund, Klaus Zwicker, Vivek Sharma, Volker Zickermann, Heike Angerer
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-8 (2020)
Respiratory complex I plays a key role in energy metabolism. Cryo-EM structure of a mutant accessory subunit LYRM6 from the yeast Yarrowia lipolytica and molecular dynamics simulations reveal conformational changes at the interface between LYRM6 and
Externí odkaz:
https://doaj.org/article/89bb52ee11ed43a19deeb0190964dfe0
Autor:
Heike Angerer
Publikováno v:
Biology, Vol 4, Iss 1, Pp 133-150 (2015)
In eukaryotic cells, mitochondria host ancient essential bioenergetic and biosynthetic pathways. LYR (leucine/tyrosine/arginine) motif proteins (LYRMs) of the Complex1_LYR-like superfamily interact with protein complexes of bacterial origin. Many LYR
Externí odkaz:
https://doaj.org/article/48b7c897257645229c189c70e287523f
Autor:
Hamid R. Nasiri, Karina Tuz, Iris Bischoff, Robert Fürst, Zhenyu Han, Oscar Juárez, Yihan Qin, Günter Fritz, Heike Angerer, Dana Lashley, Dennis P. Stegmann
Publikováno v:
ChemMedChem. 15(24)
A short, efficient one-step synthesis of 2-methyl-5-(3-methyl-2-butenyl)-1,4-benzoquinone, a natural product from Pyrola media is described. The synthesis is based on a direct late C-H functionalization of the quinone scaffold. The formation of the n
Autor:
Heike Angerer, Michael Karas, Nina Morgner, Ute Bahr, Jan Hoffmann, Juliana Heidler, Stefan Schönborn, Volker Zickermann, Ilka Wittig, Jan Gorka
Publikováno v:
Biochimica et biophysica acta. Molecular cell research. 1864(10)
The mitochondrial acyl carrier protein (ACPM/NDUFAB1) is a central element of the mitochondrial fatty acid synthesis type II machinery. Originally ACPM was detected as a subunit of respiratory complex I but the reason for the association with the lar
Autor:
Rosemary A. Stuart, Juliana Heidler, Heike Angerer, Valentina Strecker, Cristina-Maria Cruciat, Kathy Pfeiffer, Zibirnisa Kadeer, Heiko Giese, Ilka Wittig
Publikováno v:
Biochimica et biophysica acta. 1863(7 Pt)
Here we identified a hydrophobic 6.4 kDa protein, Cox26, as a novel component of yeast mitochondrial supercomplex comprising respiratory complexes III and IV. Multi-dimensional native and denaturing electrophoretic techniques were used to identify pr
Autor:
Michael Radermacher, Lucie Sokolova, Zibiernisha Wumaier, Mirco Steger, Esther Nübel, Heinrich Heide, Ulrich Brandt, Klaus Zwicker, Heike Angerer, Bernhard Brutschy, Volker Zickermann, Silke Kaiser
Publikováno v:
Biochemical Journal. 437:279-288
Mitochondrial NADH:ubiquinone oxidoreductase (complex I) is a very large membrane protein complex with a central function in energy metabolism. Complex I from the aerobic yeast Yarrowia lipolytica comprises 14 central subunits that harbour the bioene
Autor:
Jessica H. van Wonderen, Iris von der Hocht, Hartmut Michel, Heike Angerer, Florian Hilbers, Fraser MacMillan
Publikováno v:
Proceedings of the National Academy of Sciences. 108:3964-3969
Cytochrome c oxidase (C c O) is the terminal enzyme of the respiratory chain. This redox-driven proton pump catalyzes the four-electron reduction of molecular oxygen to water, one of the most fundamental processes in biology. Elucidation of the inter
Autor:
Juliane Heidler, Ilka Wittig, Heike Angerer, Karin Siegmund, Klaus Zwicker, Etienne Galemou Yoga, Volker Zickermann
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1859:e38
Autor:
Hartmut Michel, Hannelore Müller, Elena Olkhova, Bernd Ludwig, Juergen Koepke, Guohong Peng, Heike Angerer, Petra Hellwig, Katharina L. Dürr, Oliver-Matthias H. Richter
Publikováno v:
Journal of Molecular Biology. 384:865-877
Asparagine 131, located near the cytoplasmic entrance of the D-pathway in subunit I of the Paracoccus denitrificans aa(3) cytochrome c oxidase, is a residue crucial for proton pumping. When replaced by an aspartate, the mutant enzyme is completely de
Publikováno v:
FEBS Letters. 580:1345-1349
The mechanism of electron coupled proton transfer in cytochrome c oxidase (CcO) is still poorly understood. The PM-intermediate of the catalytic cycle is an oxoferryl state whose generation requires one additional electron, which cannot be provided b