Zobrazeno 1 - 10
of 33
pro vyhledávání: '"ANNE-MARIE COLSON"'
Autor:
Brigitte Meunier, Ulrich Brandt, Claus Ortwein, Peter R. Rich, Anne-Marie Colson-Corbisier, Thomas A. Link
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1321:79-92
Four point mutations in subunit I of cytochrome c oxidase from Saccharomyces cerevisiae that had been selected for respiratory incompetence but still contained spectrally detectable haem aa(3) were analysed. The isolated mutant enzymes exhibited mino
Autor:
Anne-Marie Colson, Brigitte Meunier
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1187:112-115
Publikováno v:
FEBS Letters. 339:1-6
Four modified cytochrome b's carrying mononucleotide substitutions affecting center N residues were analysed. The mutant carrying a G33D change does not incorporate heme into the apocytochrome b and fails to grow on non-fermentable carbon sources. Ou
Publikováno v:
Journal of Biological Chemistry. 269:4221-4226
A total of 110 revertants have been isolated from two well-characterized cytochrome b deficient (mit-) mutants. The mit- mutations are located in an extramembranous loop linking the transmembrane alpha-helices IV and V of cytochrome b which has been
Publikováno v:
European Journal of Biochemistry. 213:137-145
A technique has been developed for the direct analysis by visible spectrophotometry of yeast spots growing on agar plates. This allows rapid semi-quantitative estimations of cytochromes c, b and oxidase and permits the identification of strains with
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)
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1101:157-161
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1101:157-161
Publikováno v:
FEBS Letters. 278:26-30
Inbc complexes, cytochromeb plays a major role in electron transfer and in proton translocation accross the membrane. Several inhibitor-resistant and respiratory-deficient mutants have already been used to study the structure-function relationships o
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1253:13-15
Second-site revertants were selected from a respiratory-deficient mutant carrying the mutation D369N located in a loop between helices IX and X close to H376 and H378, the proposed ligands of haem a(3) and haem a, respectively. A reversion was observ