Saccharomyces cerevisiae cytochrome

K79A Saccharomyces cerevisiae cytochrome c has been carried out. RDCs due to field-induced orientation of oxidized-K79A and reduced cytochrome c at pH 7.0 and oxidized-K79A cytochrome c at pH 11.1 have been determined through measurements of amide couplings at 800 and 500 MHz. The... 

Callen DF, Wolf CR, Philpot RM. 1980. Cytochrome P-450-mediated genetic activity and cytotoxicity of seven halogenated aliphatic hydrocarbons in Saccharomyces cerevisiae. Mutat Res 77 55-63. 

King DJ, MR Azari, A Wiseman (1984) Studies on the properties of highly purified cytochrome P-448 and its dependent activity benzo[a]pyrene hydroxylase, from Saccharomyces cerevisiae. Xenobiotica 14 187-206. 

A cytochrome P450 has been purified from Saccharomyces cerevisiae that has benzo[a]pyrene hydroxylase activity (King et al. 1984), and metabolizes benzo[fl]pyrene to 3- and 9-hydroxybenzo[fl]pyrene and benzo[fl]pyrene-7,8-dihydrodiol (Wiseman and Woods 1979). The transformation of PAHs by Candida Upolytica produced predominantly monohydroxyl-ated products naphth-l-ol from naphthalene, 4-hydroxybiphenyl from biphenyl and 3- and 9-hydroxybenzo[fl]pyrene from benzo[fl]pyrene (Cerniglia and Crow 1981). The transformation of phenanthrene was demonstrated in a number of yeasts isolated from littoral sediments and of these, Trichosporumpenicillatum was the most active. In contrast, biotransformation of benz[fl]anthracene by Candida krusei and Rhodotorula minuta was much slower (MacGillivray and Shiaris 1993). 

Hunte, C., Koepke, J., Lange, C., Rossmanith, T. and Michel, H. (2000) Structure at 2.3 A resolution of the cytochrome bcj complex from the yeast Saccharomyces cerevisiae with an antibody Fv fragment, Structure, 8, 669-684. 

Cytochrom c Peroxidase [13] Saccharomyces cerevisiae 2Cc(II) + H2O2 2Cc(III) + 2H2O Reduction of H2O2 and oxidation of Cytochrom c... 

Lewis, D. F. V., Wiseman, A., and Tarbit, M. H. (1999) Molecular modeling of lanosterol 14-alpha-demethylase (CYP51) from Saccharomyces cerevisiae via homology with CYP102, a unique bacterial cytochrome P450 isoform quantitative structure-activity relationships (QSARs) within two related series of antifungal azole derivatives../. Enz. Inhib. 14, 175-192. 

Budavari, S., ed. (1996) The Merck Index, 12th Ed., Whitehouse Station, NJ, Merck Co., p. 297 Callen, D.F., Wolf, C.R. Philpot, R.M. (1980) Cytochrome P-450 mediated genetic activity and cytotoxicity of seven halogenated aliphatic hydrocarbons in Saccharomyces cerevisiae. 

Forsburg, S. L., and L. Guarente, Communication between mitochondria and the nucleus in regulation of cytochrome genes in the yeast Saccharomyces cerevisiae. Ann. Rev. Cell. Biol. 5 153-180, 1989. 

HAUDENSCHILD, C., SCHALK, M., KARP, F., CROTEAU, R. Functional expression of regiospecific cytochrome P450 limonene hydroxylases from mint (Mentha spp.) in Escherichia coli and Saccharomyces cerevisiae, Arch. Biochem. Biophys., 2000,379, 127-136. 

Flavocytochrome b2 from Saccharomyces cerevisiae, a member of the FMN-dependent oxidoreductase superfamily, catalyzes the two-electron oxidation of lactate to pyruvate with subsequent electron-transfer to cytochrome c via the bound flavin [55], What distinguishes the enzyme from other family members is the N-terminal fusion of a heme-binding domain to the ySa-barrel structure, which hosts the primary active site. Rather than dumping the electrons from the reduced flavin hydroquinone onto molecular oxygen, they are transferred intramolecularly to the heme-binding domain and from there in a second intermolecular step to cytochrome c. 

Coxl7, an 8.1-kDa cysteine-rich protein, was the first copper chaperone to be identified. Saccharomyces cerevisiae harboring mutations in coxl 7 are respiratory deficient, a phenotype resulting from their inability to assemble a functional cytochrome c oxidase complex (Glerum et al., 1996a). coxl7 mutant yeast are, however, able to express all the subunits of the cytochrome c oxidase complex, indicating that the lesion must lie in a posttranslational step that is essential for assembly of the functional complex in the mitochondrial membrane. Unlike other cytochrome c... 

FCB2 from Saccharomyces cerevisiae catalyzes the oxidation of lactic acid to pyruvic acid with subsequent transfer of two electrons to cytochrome c (Lederer, 1991). The enzyme is located in the intermembrane space of yeast mitochondria and is part of an independent branch of the... 

Flavocytochromes 2 2-hydroxyacid dehydrogenases found in the inter-membrane space of yeast mitochondria where they couple oxidation of the substrate to reduction of cytochrome c. Examples include the enzymes from Saccharomyces cerevisiae and Hansenula anomala, both of which are l-lactate dehydrogenases (Chapman et al., 1998), and the enzyme from Rhodotorula graminis which is a L-mandelate dehydrogenase (Ilias et al., 1998). This article will concentrate on the flavocytochrome 2 (L-lactate cytochrome c oxidoreductase) from S. cerevisiae (Bakersi yeast), since this is by far the most studied of these enzymes (Chapman et al., 1991). Therefore, throughout this article, the term flavocytochrome 2 will refer specifically to the enzyme from S. cerevisiae unless otherwise stated. 

Sakaki, T., Shibata, M., Yabusaki, Y., Murakami, H., and Ohkawa, H., 1990, Expression of bovine cytochrome P450c21 and its fused enzymes with yeast NADPH-cytochrome P450 reductase in Saccharomyces cerevisiae, DNA Cell Biol. 9 6039614. 

Graham, L. A., Brandt, U., Sargent, J. S., and Trumpower, B. L., 1992, Mutational analysis of assembly and function of the iron-suUur protein of the cytochrome fcc, complex in saccharomyces cerevisiae, J. Bioenerg. Biomembr. 25 245n257. 

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