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Volumn 43, Issue 39, 2004, Pages 12390-12409

Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP: Biophysical properties and interactions with cytochrome P450 bioI

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; AMINO ACIDS; DIFFERENTIAL SCANNING CALORIMETRY; DNA; DNA SEQUENCES; ESCHERICHIA COLI; MASS SPECTROMETRY; MELTING; PURIFICATION; SUBSTRATES; THERMAL EFFECTS; TITRATION;

EID: 4744337841     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049131t     Document Type: Article
Times cited : (76)

References (59)
  • 1
    • 0345257913 scopus 로고    scopus 로고
    • Multiple oxidants and multiple mechanisms in cytochrome P450 catalysis
    • Coon, M. J. (2003) Multiple oxidants and multiple mechanisms in cytochrome P450 catalysis, Biochem. Biophys. Res. Commun. 312, 163-168.
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 163-168
    • Coon, M.J.1
  • 2
    • 0038541790 scopus 로고    scopus 로고
    • Haemoxygen reactive intermediates: Catalysis by the two-step
    • Makris, T. M., Denisov, I. G., and Sligar, S. G. (2003) Haemoxygen reactive intermediates: catalysis by the two-step, Biochem. Soc. Trans. 31, 516-519.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 516-519
    • Makris, T.M.1    Denisov, I.G.2    Sligar, S.G.3
  • 3
    • 0037960909 scopus 로고    scopus 로고
    • Can a single oxidant with two spin states masquerade as two different oxidants? A study of the sulfoxidation mechanism by cytochrome P450
    • Sharma, P. K., De Visser, S. P., and Shaik, S. (2003) Can a single oxidant with two spin states masquerade as two different oxidants? A study of the sulfoxidation mechanism by cytochrome P450, J. Am. Chem. Soc. 125, 8698-8699.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8698-8699
    • Sharma, P.K.1    De Visser, S.P.2    Shaik, S.3
  • 4
    • 0141869098 scopus 로고    scopus 로고
    • Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida
    • Sevrioukova, I. F., Garcia, C., Li, H., Bhaskar, B., and Poulos, T. L. (2003) Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida, J. Mol. Biol. 333, 377-392.
    • (2003) J. Mol. Biol. , vol.333 , pp. 377-392
    • Sevrioukova, I.F.1    Garcia, C.2    Li, H.3    Bhaskar, B.4    Poulos, T.L.5
  • 5
    • 0025257597 scopus 로고
    • Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins
    • Peterson, J. A., Lorence, M. C., and Amarneh, B. (1990) Putidaredoxin reductase and putidaredoxin. Cloning, sequence determination, and heterologous expression of the proteins, J. Biol. Chem. 265, 6066-6073.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6066-6073
    • Peterson, J.A.1    Lorence, M.C.2    Amarneh, B.3
  • 6
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
    • Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S., and Kim, J. J. (1997) Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes, Proc. Natl. Acad. Sci. U.S.A. 94, 8411-8416.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.5    Kim, J.J.6
  • 7
    • 0035800760 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer
    • Hubbard, P. A., Shen, A. L., Paschke, R., Kasper, C. B., and Kim, J. J. (2001) NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer, J. Biol. Chem. 276, 29163-29170.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29163-29170
    • Hubbard, P.A.1    Shen, A.L.2    Paschke, R.3    Kasper, C.B.4    Kim, J.J.5
  • 8
    • 0035916295 scopus 로고    scopus 로고
    • Determination of the redox properties of human NADPH-cytochrome P450 reductase
    • Munro, A. W., Noble, M. A., Robledo, L., Daff, S. N., and Chapman, S. K. (2001) Determination of the redox properties of human NADPH-cytochrome P450 reductase, Biochemistry 40, 1956-1963.
    • (2001) Biochemistry , vol.40 , pp. 1956-1963
    • Munro, A.W.1    Noble, M.A.2    Robledo, L.3    Daff, S.N.4    Chapman, S.K.5
  • 9
    • 0037046154 scopus 로고    scopus 로고
    • Relaxation kinetics of cytochrome P450 reductase: Internal electron transfer is limited by conformational change and regulated by coenzyme binding
    • Gutierrez, A., Paine, M., Wolf, C. R., Scrutton, N. S., and Roberts, G. C. K. (2002) Relaxation kinetics of cytochrome P450 reductase: internal electron transfer is limited by conformational change and regulated by coenzyme binding, Biochemistry 41, 4626-4637.
    • (2002) Biochemistry , vol.41 , pp. 4626-4637
    • Gutierrez, A.1    Paine, M.2    Wolf, C.R.3    Scrutton, N.S.4    Roberts, G.C.K.5
  • 10
    • 0023806175 scopus 로고
    • Characterization of the protein expressed in Escherichia coli by a recombinant plasmid containing the Bacillus megaterium cytochrome P-450 BM-3 gene
    • Narhi, L. O., Wen, L. P., and Fulco, A. J. (1988) Characterization of the protein expressed in Escherichia coli by a recombinant plasmid containing the Bacillus megaterium cytochrome P-450 BM-3 gene, Mol. Cell. Biochem. 79, 63-71.
    • (1988) Mol. Cell. Biochem. , vol.79 , pp. 63-71
    • Narhi, L.O.1    Wen, L.P.2    Fulco, A.J.3
  • 11
    • 0025922972 scopus 로고
    • P450 BM-3 and other inducible bacterial P450 cytochromes: Biochemistry and regulation
    • Fulco, A. J. (1991) P450 BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation, Annu. Rev. Pharmacol. Toxicol. 31, 177-203.
    • (1991) Annu. Rev. Pharmacol. Toxicol. , vol.31 , pp. 177-203
    • Fulco, A.J.1
  • 13
    • 0034739049 scopus 로고    scopus 로고
    • Crystal structures of cytochrome P450nor and its mutants (Ser286 to Val, Thr) in the ferric resting state at cryogenic temperature: A comparative analysis with monooxygenase cytochrome P450s
    • Shimizu, H., Park, S., Lee, D., Shoun, H., and Shiro, Y. (2000) Crystal structures of cytochrome P450nor and its mutants (Ser286 to Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s, J. Inorg. Biochem. 81, 191-205.
    • (2000) J. Inorg. Biochem. , vol.81 , pp. 191-205
    • Shimizu, H.1    Park, S.2    Lee, D.3    Shoun, H.4    Shiro, Y.5
  • 14
    • 0037646516 scopus 로고    scopus 로고
    • Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies
    • Lee, D. S., Yamada, A., Sugimoto, H., Matsunaga, I., Ogura, H., Ichihara, K., Adachi, S., Park, S. Y., and Shiro, Y. (2003) Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies, J. Biol. Chem. 278, 9761-9767.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9761-9767
    • Lee, D.S.1    Yamada, A.2    Sugimoto, H.3    Matsunaga, I.4    Ogura, H.5    Ichihara, K.6    Adachi, S.7    Park, S.Y.8    Shiro, Y.9
  • 15
    • 0036299635 scopus 로고    scopus 로고
    • Identification of a new class of cytochrome P450 from a Rhodococcus sp
    • Roberts, G. A., Grogan, G., Greter, A., Flitsch, S. L., and Turner, N. J. (2002) Identification of a new class of cytochrome P450 from a Rhodococcus sp, J. Bacteriol. 184, 3898-3908.
    • (2002) J. Bacteriol. , vol.184 , pp. 3898-3908
    • Roberts, G.A.1    Grogan, G.2    Greter, A.3    Flitsch, S.L.4    Turner, N.J.5
  • 16
    • 0034846763 scopus 로고    scopus 로고
    • Expression, purification and characterization of cytochrome P450 BioI: A novel P450 involved in biotin synthesis in Bacillus subtilis
    • Green, A. J., Rivers, S. L., Cheesman, M. R., Reid, G. A., Quaroni, L. G., Macdonald, I. D. G., Chapman, S. K., and Munro, A. W. (2001) Expression, purification and characterization of cytochrome P450 BioI: a novel P450 involved in biotin synthesis in Bacillus subtilis, J. Biol. Inorg. Chem. 6, 523-533.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 523-533
    • Green, A.J.1    Rivers, S.L.2    Cheesman, M.R.3    Reid, G.A.4    Quaroni, L.G.5    Macdonald, I.D.G.6    Chapman, S.K.7    Munro, A.W.8
  • 17
    • 0037245378 scopus 로고    scopus 로고
    • Expression, purification and characterisation of a Bacillus subtilis ferredoxin: A potential electron transfer donor to cytochrome P450 BioI
    • Green, A. J., Munro, A. W., Cheesman, M. R., Reid, G. A., von Wachenfeldt, C., and Chapman, S. K. (2003) Expression, purification and characterisation of a Bacillus subtilis ferredoxin: a potential electron transfer donor to cytochrome P450 BioI. J. Inorg. Biochem. 93, 92-99.
    • (2003) J. Inorg. Biochem. , vol.93 , pp. 92-99
    • Green, A.J.1    Munro, A.W.2    Cheesman, M.R.3    Reid, G.A.4    Von Wachenfeldt, C.5    Chapman, S.K.6
  • 18
    • 0035965284 scopus 로고    scopus 로고
    • The interaction of bovine adrenodoxin with CYP11A1 (cytochrome P450scc) and CYP11B1 (cytochrome P45011β). Acceleration of reduction and substrate conversion by site-directed mutagenesis of adrenodoxin
    • Schiffler, B., Kiefer, M., Wilken, A., Hannemann, F., Adolph, H. W., and Bernhardt, R. (2001) The interaction of bovine adrenodoxin with CYP11A1 (cytochrome P450scc) and CYP11B1 (cytochrome P45011β). Acceleration of reduction and substrate conversion by site-directed mutagenesis of adrenodoxin, J. Biol. Chem. 276, 36225-36232.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36225-36232
    • Schiffler, B.1    Kiefer, M.2    Wilken, A.3    Hannemann, F.4    Adolph, H.W.5    Bernhardt, R.6
  • 19
    • 0032997283 scopus 로고    scopus 로고
    • Cloning and characterization of the genes encoding a cytochrome P450 (PipA) involved in piperidine and pyrrolidine utilization and its regulatory protein (PipR) in Mycobacterium smegmatis mc2155
    • Poupin, P., Ducrocq, V., Hallier-Soulier, S., and Truffaut, N. (1999) Cloning and characterization of the genes encoding a cytochrome P450 (PipA) involved in piperidine and pyrrolidine utilization and its regulatory protein (PipR) in Mycobacterium smegmatis mc2155, J. Bacteriol. 181, 3419-3426.
    • (1999) J. Bacteriol. , vol.181 , pp. 3419-3426
    • Poupin, P.1    Ducrocq, V.2    Hallier-Soulier, S.3    Truffaut, N.4
  • 20
    • 0030731108 scopus 로고    scopus 로고
    • The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
    • Kunst, K., Ogasawara, N., Moszer, I., Albertini, A. M., Azevedo, V., et al. (1997) The complete genome sequence of the Gram-positive bacterium Bacillus subtilis, Nature 390, 249-256.
    • (1997) Nature , vol.390 , pp. 249-256
    • Kunst, K.1    Ogasawara, N.2    Moszer, I.3    Albertini, A.M.4    Azevedo, V.5
  • 21
    • 0034671777 scopus 로고    scopus 로고
    • Expression, purification, and characterization of BioI: A carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis
    • Stok, J. E., and De Voss, J. (2000) Expression, purification, and characterization of BioI: a carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis, Arch. Biochem. Biophys. 384, 351-360.
    • (2000) Arch. Biochem. Biophys. , vol.384 , pp. 351-360
    • Stok, J.E.1    De Voss, J.2
  • 22
    • 0141632672 scopus 로고    scopus 로고
    • Products of cytochrome P450 BioI (CYP107H1)-catalyzed oxidation of fatty acids
    • Cryle, M. J., Matovic, N. J., and De Voss, J. J. (2003) Products of cytochrome P450 BioI (CYP107H1)-catalyzed oxidation of fatty acids, Org. Lett. 5, 3341-334.
    • (2003) Org. Lett. , vol.5 , pp. 3341-3334
    • Cryle, M.J.1    Matovic, N.J.2    De Voss, J.J.3
  • 25
    • 0000323018 scopus 로고
    • General properties of flavodoxins
    • (Müller, F., Ed.), CRC Press, Boca Raton
    • Mayhew, S. G., and Tollin, G. (1992) General properties of flavodoxins, in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.), Vol. III, pp 389-426, CRC Press, Boca Raton, FL.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 389-426
    • Mayhew, S.G.1    Tollin, G.2
  • 26
    • 0017626285 scopus 로고
    • Activation of methionine synthase: A further characterization of the flavoprotein system
    • Fujii, K., Galivan, J. H., and Hennekens, F. M. (1977) Activation of methionine synthase: A further characterization of the flavoprotein system, Arch. Biochem. Biophys. 178, 662-670.
    • (1977) Arch. Biochem. Biophys. , vol.178 , pp. 662-670
    • Fujii, K.1    Galivan, J.H.2    Hennekens, F.M.3
  • 28
    • 0020064853 scopus 로고
    • Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate:flavodoxin and NADPH: Flavodoxin oxidoreductases participating in the activation of pyruvate-formate lyase
    • Blaschkowski, H. P., Neuer, G., Ludwig-Festl, M., and Knappe, J. (1982) Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate:flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate-formate lyase, Eur. J. Biochem. 123, 563-569.
    • (1982) Eur. J. Biochem. , vol.123 , pp. 563-569
    • Blaschkowski, H.P.1    Neuer, G.2    Ludwig-Festl, M.3    Knappe, J.4
  • 29
    • 0346727529 scopus 로고    scopus 로고
    • Crystal structure of biotin synthase, an S-adenosyl-methionine-dependent radical enzyme
    • Berkovitch, F., Nicolet, Y., Wan, J. T., Jarrett, J. T., and Drennan, C. L. (2004) Crystal structure of biotin synthase, an S-adenosyl-methionine- dependent radical enzyme, Science 303, 76-79.
    • (2004) Science , vol.303 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 30
    • 0002714616 scopus 로고
    • Structure and redox properties of clostridial flavodoxin
    • (Müller, F., Ed.), CRC Press, Boca Raton, FL
    • Ludwig, M., and Luschinsky, C. L. (1992) Structure and redox properties of clostridial flavodoxin, in Chemistry and Biochemistry of Flavoenzymes (Müller, F., Ed.) Vol. III, pp 427-466, CRC Press, Boca Raton, FL.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 427-466
    • Ludwig, M.1    Luschinsky, C.L.2
  • 31
    • 0036035079 scopus 로고    scopus 로고
    • Global analysis of the Bacillus subtilus fur regulon and the iron starvation stimulon
    • Baichoo, N., Wang, T., Ye, R., and Helmann, J. D. (2002) Global analysis of the Bacillus subtilus Fur regulon and the iron starvation stimulon, Mol. Microbiol. 45, 1613-1629.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1613-1629
    • Baichoo, N.1    Wang, T.2    Ye, R.3    Helmann, J.D.4
  • 33
    • 0029047343 scopus 로고
    • Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro
    • Birch, O. M., Fuhrmann, M., and Shaw, N. M. (1995) Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro, J. Biol. Chem. 270, 19158-19165.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19158-19165
    • Birch, O.M.1    Fuhrmann, M.2    Shaw, N.M.3
  • 37
    • 0025741770 scopus 로고
    • Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: Purification and characterization
    • Macheroux P., Massey V., Thiele D. J., and Volokita M. (1991) Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: purification and characterization, Biochemistry 30, 4612-4619.
    • (1991) Biochemistry , vol.30 , pp. 4612-4619
    • Macheroux, P.1    Massey, V.2    Thiele, D.J.3    Volokita, M.4
  • 38
    • 0016559305 scopus 로고
    • Fluorescence titration with apoflavodoxin: A sensitive assay for riboflavin 5′-phosphate and flavin adenine dinucleotide in mixtures
    • Wassink, J. H., and Mayhew, S. G. (1975) Fluorescence titration with apoflavodoxin: a sensitive assay for riboflavin 5′-phosphate and flavin adenine dinucleotide in mixtures, Anal. Biochem. 68, 609-616.
    • (1975) Anal. Biochem. , vol.68 , pp. 609-616
    • Wassink, J.H.1    Mayhew, S.G.2
  • 39
    • 0034660451 scopus 로고    scopus 로고
    • No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin
    • Apiyo, D., Guidty, J., and Wittung-Stafshede, P. (2000) No cofactor effect on equilibrium unfolding of Desulfovibrio desulfuricans flavodoxin, Biochim. Biophys. Acta 1479, 214-224.
    • (2000) Biochim. Biophys. Acta , vol.1479 , pp. 214-224
    • Apiyo, D.1    Guidty, J.2    Wittung-Stafshede, P.3
  • 40
    • 0030065530 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of the binding of riboflavin, riboflavin 5′-phosphate and riboflavin 3′, 5′-bisphosphate by apoflavodoxins
    • Pueyo, J. J., Curley, G. P., and Mayhew, S. G. (1996) Kinetics and thermodynamics of the binding of riboflavin, riboflavin 5′-phosphate and riboflavin 3′, 5′-bisphosphate by apoflavodoxins, Biochem. J. 313, 855-861.
    • (1996) Biochem. J. , vol.313 , pp. 855-861
    • Pueyo, J.J.1    Curley, G.P.2    Mayhew, S.G.3
  • 42
    • 0018115502 scopus 로고
    • Redox potentiometry: Determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems
    • Dutton, P. L. (1978) Redox potentiometry: determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems, Methods Enzymol. 54, 411-435.
    • (1978) Methods Enzymol. , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 43
    • 0031454750 scopus 로고    scopus 로고
    • A flavodoxin that is required for enzyme activation: The structure of oxidized flavodoxin from Escherichia coli at 1.8 Å resolution
    • Hoover, D. M., and Ludwig, M. L. (1997) A flavodoxin that is required for enzyme activation: The structure of oxidized flavodoxin from Escherichia coli at 1.8 Å resolution, Protein Sci. 6, 2525-2537.
    • (1997) Protein Sci. , vol.6 , pp. 2525-2537
    • Hoover, D.M.1    Ludwig, M.L.2
  • 45
    • 0037418539 scopus 로고    scopus 로고
    • Mechanism of flavin mononucleotide cofactor binding to the Desulfovibrio vulgaris flavodoxin. 1. Kinetic evidence for cooperative effects associated with the binding of inorganic phosphate and the 5′-phosphate moiety of the cofactor
    • Arnold Murray, T., and Swenson, R. P. (2003) Mechanism of flavin mononucleotide cofactor binding to the Desulfovibrio vulgaris flavodoxin. 1. Kinetic evidence for cooperative effects associated with the binding of inorganic phosphate and the 5′-phosphate moiety of the cofactor, Biochemistry 42, 2307-2316.
    • (2003) Biochemistry , vol.42 , pp. 2307-2316
    • Arnold Murray, T.1    Swenson, R.P.2
  • 46
    • 0033152446 scopus 로고    scopus 로고
    • The midpoint potential for the oxidized-semiquinone couple for Gly57 mutants of the Clostridium beijerinkii flavodoxin correlate with changes in the hydrogen-bonding interaction with the proton on N5 of the reduced flavin mononucleotide cofactor as measured by NMR chemical shift temperature dependencies
    • Chang, F.-C., and Swenson, R. P. (1999) The midpoint potential for the oxidized-semiquinone couple for Gly57 mutants of the Clostridium beijerinkii flavodoxin correlate with changes in the hydrogen-bonding interaction with the proton on N5 of the reduced flavin mononucleotide cofactor as measured by NMR chemical shift temperature dependencies, Biochemistry 38, 7168-7176.
    • (1999) Biochemistry , vol.38 , pp. 7168-7176
    • Chang, F.-C.1    Swenson, R.P.2
  • 48
    • 0015220750 scopus 로고
    • Studies on flavin binding in flavodoxins
    • Mayhew, S. G. (1971) Studies on flavin binding in flavodoxins, Biochim. Biophys. Acta 235, 289-302.
    • (1971) Biochim. Biophys. Acta , vol.235 , pp. 289-302
    • Mayhew, S.G.1
  • 49
    • 0026351132 scopus 로고
    • Redox and flavin-binding properties of recombinant flavodoxin from Desulfovibrio vulgaris (Hildenborough)
    • Curley, G. P., Carr, M. C., Mayhew, S. G., and Voordouw, G. (1991) Redox and flavin-binding properties of recombinant flavodoxin from Desulfovibrio vulgaris (Hildenborough), Eur. J. Biochem. 202, 1091-1100.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1091-1100
    • Curley, G.P.1    Carr, M.C.2    Mayhew, S.G.3    Voordouw, G.4
  • 50
    • 0036156208 scopus 로고    scopus 로고
    • A comparison of the urea-induced unfolding of apoflavodoxin and flavodoxin from Desulfovibrio vulgaris
    • Nuallain, B. O., and Mayhew, S. G. (2002) A comparison of the urea-induced unfolding of apoflavodoxin and flavodoxin from Desulfovibrio vulgaris, Eur. J. Biochem. 269, 212-223.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 212-223
    • Nuallain, B.O.1    Mayhew, S.G.2
  • 51
    • 0020465726 scopus 로고
    • Equilibrium and kinetic studies of the interaction of cytochrome P-450cam and putidaredoxin
    • Hintz, J. M., Mock, D. M., Peterson, L. L., Tuttle, K., and Peterson, J. A. (1982) Equilibrium and kinetic studies of the interaction of cytochrome P-450cam and putidaredoxin, J. Biol. Chem. 257, 14324-14332.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14324-14332
    • Hintz, J.M.1    Mock, D.M.2    Peterson, L.L.3    Tuttle, K.4    Peterson, J.A.5
  • 52
    • 0036130402 scopus 로고    scopus 로고
    • Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase
    • Beaman, T. W., Vogel, K. W., Drueckhammer, D. G., Blanchard, J. S., and Roderick, S. L. (2002) Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase, Protein Sci. 11, 974-979.
    • (2002) Protein Sci. , vol.11 , pp. 974-979
    • Beaman, T.W.1    Vogel, K.W.2    Drueckhammer, D.G.3    Blanchard, J.S.4    Roderick, S.L.5
  • 53
    • 1242318677 scopus 로고    scopus 로고
    • Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress
    • Mostertz, J., Scharf, C., Hecker, M., and Homuth, G. (2004) Transcriptome and proteome analysis of Bacillus subtilis gene expression in response to superoxide and peroxide stress, Microbiology 150, 497-512.
    • (2004) Microbiology , vol.150 , pp. 497-512
    • Mostertz, J.1    Scharf, C.2    Hecker, M.3    Homuth, G.4
  • 55
    • 0015220756 scopus 로고
    • Properties of two clostridial flavodoxins
    • Mayhew, S. G. (1971) Properties of two clostridial flavodoxins, Biochim. Biophys. Acta 235, 276-288.
    • (1971) Biochim. Biophys. Acta , vol.235 , pp. 276-288
    • Mayhew, S.G.1
  • 56
    • 0033563872 scopus 로고    scopus 로고
    • P450 BM3: Absolute configuration of the primary metabolites of palmitic acid
    • Truan, G., Komandla, M. R., Falck, J. R., and Peterson, J. A. (1999) P450 BM3: absolute configuration of the primary metabolites of palmitic acid, Arch. Biochem. Biophys. 366, 192-198.
    • (1999) Arch. Biochem. Biophys. , vol.366 , pp. 192-198
    • Truan, G.1    Komandla, M.R.2    Falck, J.R.3    Peterson, J.A.4
  • 57
    • 1642458263 scopus 로고    scopus 로고
    • Carbon-carbon bond cleavage by cytochrome P450 BioI (CYP107H1)
    • Cryle, M. J., and De Voss, J. J. (2004) Carbon-carbon bond cleavage by cytochrome P450 BioI (CYP107H1), Chem. Commun. 86, 86-87.
    • (2004) Chem. Commun. , vol.86 , pp. 86-87
    • Cryle, M.J.1    De Voss, J.J.2
  • 59
    • 0015210971 scopus 로고
    • Flavoprotein chemistry. I. Circular dichroism studies of the flavin chromophore and the relation between redox properties and flavin environment in oxidases and dehydrogenases
    • Edmondson, D. E., and Tollin, G. (1971) Flavoprotein chemistry. I. Circular dichroism studies of the flavin chromophore and the relation between redox properties and flavin environment in oxidases and dehydrogenases, Biochemistry 10, 113-124.
    • (1971) Biochemistry , vol.10 , pp. 113-124
    • Edmondson, D.E.1    Tollin, G.2


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