CYB2/YML054C Literature Guide Help

Other names published for CYB2: FCB2, YML054C

CYB2 - Protein Physical Properties (21)

ReferenceOther Genes Addressed
Melnikov D, et al.  (2010) Enzymatic AND logic gates operated under conditions characteristic of biomedical applications. J Phys Chem B 114(37):12166-74
Rintala E, et al.  (2009) Low oxygen levels as a trigger for enhancement of respiratory metabolism in Saccharomyces cerevisiae. BMC Genomics 10():461
Boubacar AK, et al.  (2007) Flavocytochrome b(2): Reactivity of Its Flavin with Molecular Oxygen. Biochemistry 46(45):13080-8
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
Le KH, et al.  (2003) Epitope mapping for the monoclonal antibody that inhibits intramolecular electron transfer in flavocytochrome b2. Biochem J 373(Pt 1):115-23
Salusjarvi L, et al.  (2003) Proteome analysis of recombinant xylose-fermenting Saccharomyces cerevisiae. Yeast 20(4):295-314
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
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
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
Lederer F  (1992) Extreme pKa displacements at the active sites of FMN-dependent alpha-hydroxy acid-oxidizing enzymes. Protein Sci 1(4):540-8
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
Sturtevant JM and Tsong TY  (1969) Investigations of yeast L-lactate dehydrogenase (cytochrome b2). VI. Circular dichroism of the holoenzyme. J Biol Chem 244(18):4942-50
Tsong TY and Sturtevant JM  (1969) Investigations of yeast L-lactate dehydrogenase (cytochrome b2). V. Circular dichroism of the flavin mononucleotide-free apoenzyme. J Biol Chem 244(9):2397-402
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
CREMONA T and SINGER TP  (1964) THE LACTIC DEHYDROGENASES OF YEAST. V. CHEMICAL PROPERTIES AND FUNCTION OF THE ZINC COMPONENT OF D-LACTIC CYTOCHROME REDUCTASE. J Biol Chem 239():1466-73
MORTON RK and STURTEVANT JM  (1964) KINETIC INVESTIGATIONS OF YEAST L-LACTATE DEHYDROGENASE (CYTOCHROME B2). I. THE DEHYDROGENATION OF L-LACTATE IN THE PRESENCE AND ABSENCE OF FERRICYANIDE AS ELECTRON ACCEPTOR. J Biol Chem 239:1614-24
NYGAARD AP  (1961) D- and L-Lactic cytochrome c reductases of yeast: reversible interaction of inhibitors at the active sites. J Biol Chem 236:2779-82