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Kinetic Properties and Ligand Binding of the Eleven-subunit Cytochrome-c Oxidase from Saccharomyces cerevisiae Isolated with a Novel Large-Scale Purification Method

Autor: Gebhard von Jagow, Thomas A. Link, Ulrich Brandt, B. M. Geier, Wilfred R. Hagen, Hermann Schägger, Claus Ortwein

Publikováno v: European Journal of Biochemistry. 227:296-302

A novel, large-scale method for the purification of cytochrome-c oxidase from the yeast Saccharomyces cerevisiae is described. The isolation procedure gave highly pure and active enzyme at high yields. The purified enzyme exhibited a heme a/protein r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9acfe93fc7254f1b418d06a7e2962d7c
https://doi.org/10.1111/j.1432-1033.1995.tb20388.x

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Analysis of cytochrome-b amino acid residues forming the contact face with the iron-sulfur subunit of ubiquinol:cytochrome-c reductase in Saccharomyces cerevisiae

Autor: P P Slonimski, G. von Jagow, B. M. Geier, J P de Rago, A Giessler

Publikováno v: European Journal of Biochemistry. 222:147-154

Four mutations in the mitochondrial cytochrome b of Saccharomyces cerevisiae have been characterized with respect to catalytic properties, inhibitor resistance and subunit interaction. The respiratory-deficient mutant [G137E]cytochrome b and the pseu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a431f1a7d62b66d7a98b22abf6181ca
https://doi.org/10.1111/j.1432-1033.1994.tb18852.x

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Point mutation in cytochrome b of yeast ubihydroquinone:cytochrome-c oxidoreductase causing myxothiazol resistance and facilitated dissociation of the iron-sulfur subunit

Autor: Anne-Marie Colson, Gebhard von Jagow, B. M. Geier, Ulrich Brandt, Hermann Schägger

Publikováno v: European Journal of Biochemistry. 208:375-380

Cytochrome-c reductase was isolated from Saccharomyces cerevisiae GM50-3C. A tenth subunit was detected with molecular mass 8.5 kDa on SDS/PAGE. Two yeast mutants selected for resistance to myxothiazol, an inhibitor of the Q(0) center (Q, ubiquinone)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fe430dcd9e14aaea3555b59f35f949c
https://doi.org/10.1111/j.1432-1033.1992.tb17197.x

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The mammalian mitochondrial respiratory chain

Autor: G. von Jagow, B. M. Geier, Thomas A. Link

Publikováno v: Bioenergetics ISBN: 9783034898607

Approximately 90% of the ATP synthesized in the cells of animals is supplied by oxidative phosphorylation. This process takes place at the inner mitochondrial membrane. The respiratory chain builds up an electrochemical membrane potential across the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c2646aec753e519e50cbed4c7f9b7a5e
https://doi.org/10.1007/978-3-0348-8994-0_6

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Characterization of green alga, yeast, and human centrins. Specific subdomain features determine functional diversity

Autor: H, Wiech, B M, Geier, T, Paschke, A, Spang, K, Grein, J, Steinkötter, M, Melkonian, E, Schiebel

Publikováno v: The Journal of biological chemistry. 271(37)

Centrins are a subfamily within the superfamily of Ca2+-modulated proteins that play a fundamental role in centrosome duplication and contraction of centrin-based fiber systems. We examined the individual molecular properties of yeast, green alga, an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4e9c8433fd38d9e7047eb07b7bc0668c
https://pubmed.ncbi.nlm.nih.gov/8798410

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