CYB2/YML054C Literature Guide Help

Other names published for CYB2: FCB2, YML054C

CYB2 - Function/Process (27)

ReferenceOther Genes Addressed
Banci L, et al.  (2011) Copper exposure effects on yeast mitochondrial proteome. J Proteomics 74(11):2522-35
Cenas N, et al.  (2007) Potentiometric and Further Kinetic Characterization of the Flavin-Binding Domain of Saccharomyces cerevisiae Flavocytochrome b(2). Inhibition by Anions Binding in the Active Site. Biochemistry 46(15):4661-70
Tsai CL, et al.  (2007) Mechanistic and structural studies of H373Q flavocytochrome b2: effects of mutating the active site base. Biochemistry 46(26):7844-51
Leger C, et al.  (2006) Electron flow in multicenter enzymes: theory, applications, and consequences on the natural design of redox chains. J Am Chem Soc 128(1):180-7
Grad LI, et al.  (2005) Introduction of an additional pathway for lactate oxidation in the treatment of lactic acidosis and mitochondrial dysfunction in Caenorhabditis elegans. Proc Natl Acad Sci U S A 102(51):18367-72
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Sobrado P and Fitzpatrick PF  (2003) Solvent and primary deuterium isotope effects show that lactate CH and OH bond cleavages are concerted in Y254F flavocytochrome b2, consistent with a hydride transfer mechanism. Biochemistry 42(51):15208-14
Cunane LM, et al.  (2002) Crystallographic study of the recombinant flavin-binding domain of Baker's yeast flavocytochrome b(2): comparison with the intact wild-type enzyme. Biochemistry 41(13):4264-72
Gondry M, et al.  (2001) The catalytic role of tyrosine 254 in flavocytochrome b2 (L-lactate dehydrogenase from baker's yeast). Comparison between the Y254F and Y254L mutant proteins. Eur J Biochem 268(18):4918-27
Grandier-Vazeille X, et al.  (2001) Yeast mitochondrial dehydrogenases are associated in a supramolecular complex. Biochemistry 40(33):9758-69
Sobrado P, et al.  (2001) Probing the relative timing of hydrogen abstraction steps in the flavocytochrome b2 reaction with primary and solvent deuterium isotope effects and mutant enzymes. Biochemistry 40(4):994-1001
Mowat CG, et al.  (2000) Changing the heme ligation in flavocytochrome b2: substitution of histidine-66 by cysteine. J Biol Inorg Chem 5(5):584-92
Mowat CG, et al.  (2000) Kinetic and crystallographic studies on the active site Arg289Lys mutant of flavocytochrome b2 (yeast L-lactate dehydrogenase). Biochemistry 39(12):3266-75
Ramil E, et al.  (2000) Regulation of the CYB2 gene expression: transcriptional co-ordination by the Hap1p, Hap2/3/4/5p and Adr1p transcription factors. Mol Microbiol 37(5):1116-32
Chen X, et al.  (1999) Signal peptides having standard and nonstandard cleavage sites can be processed by Imp1p of the mitochondrial inner membrane protease. J Biol Chem 274(53):37750-4
Rao KS and Lederer F  (1998) About the pKa of the active-site histidine in flavocytochrome b2 (yeast L-lactate dehydrogenase). Protein Sci 7(7):1531-7
Lodi T and Ferrero I  (1993) Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase. Mol Gen Genet 238(3):315-24
Davis ES, et al.  (1992) A yeast cyclophilin gene essential for lactate metabolism at high temperature. Proc Natl Acad Sci U S A 89(23):11169-73
Lodi T and Guiard B  (1991) Complex transcriptional regulation of the Saccharomyces cerevisiae CYB2 gene encoding cytochrome b2: CYP1(HAP1) activator binds to the CYB2 upstream activation site UAS1-B2. Mol Cell Biol 11(7):3762-72
Haumont PY, et al.  (1987) Amino-acid sequence of the cytochrome-b5-like heme-binding domain from Hansenula anomala flavocytochrome b2. Eur J Biochem 169(3):539-46
Rush K, et al.  (1986) Null and electrophoretic mobility mutants in the structural gene for L-lactate dehydrogenase of Saccharomyces cerevisiae. FEBS Lett 198(1):89-91
Urban P and Lederer F  (1985) Intermolecular hydrogen transfer catalyzed by a flavodehydrogenase, bakers' yeast flavocytochrome b2. J Biol Chem 260(20):11115-22
Pompon D, et al.  (1980) Flavocytochrome b2 (Baker's yeast). Deuterium isotope effect studied by rapid-kinetic methods as a probe for the mechanism of electron transfer. Eur J Biochem 104(2):479-88
Iwatsubo M, et al.  (1977) Rapid kinetic studies of partial reactions in the heme free derivative of L-lactate cytochrome c oxidoreductase (flavocytochrome b2); the flavodehydrogenase function. Biochemistry 16(16):3558-66
Prats M  (1977) Proteolysis of L-(+)-lactate cytochrome c oxidoreductase (cytochrome b2) extracted from Saccharomyces cerevisiae and Hansenula anomala yeasts. Eur J Biochem 75(2):619-25
Sturtevant JM and Tsong TY  (1968) Investigations of yeast L-lactate dehydrogenase (cytochrome b2). IV. Optical rotatory dispersion. J Biol Chem 243(9):2359-66
Hiromi K and Sturtevant JM  (1965) Investigations of yeast L-lactate dyhydrogenase (cytochrome b2). II. Anaerobic spectrophotometric and electron spin resonance titrations. J Biol Chem 240(12):4662-8