메뉴 건너뛰기




Volumn 45, Issue 44, 2006, Pages 13276-13283

Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CROSSLINKING; ELECTRONS; OXYGEN; REACTION KINETICS;

EID: 33750702163     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061497d     Document Type: Article
Times cited : (42)

References (26)
  • 1
    • 0025785660 scopus 로고
    • A new cofactor in a prokaryotic enzyme: Tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase
    • McIntire, W. S., Wemmer, D. E., Chistoserdov, A., and Lidstrom, M. E. (1991) A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase, Science 252, 817-824.
    • (1991) Science , vol.252 , pp. 817-824
    • McIntire, W.S.1    Wemmer, D.E.2    Chistoserdov, A.3    Lidstrom, M.E.4
  • 2
    • 0034797851 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase
    • Davidson, V. L. (2001) Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase, Adv. Protein Chem. 58, 95-140.
    • (2001) Adv. Protein Chem. , vol.58 , pp. 95-140
    • Davidson, V.L.1
  • 5
    • 0027996934 scopus 로고
    • Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator
    • Van Spanning, R. J., van der Palen, C. J., Slotboom, D. J., Reijnders, W. N., Stouthamer, A. H., and Duine, J. A. (1994) Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator, Eur. J. Biochem. 226, 201-210.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 201-210
    • Van Spanning, R.J.1    Van Der Palen, C.J.2    Slotboom, D.J.3    Reijnders, W.N.4    Stouthamer, A.H.5    Duine, J.A.6
  • 6
    • 0025149403 scopus 로고
    • Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation
    • van Spanning, R. J., Wansell, C. W., Reijnders, W. N., Oltmann, L. F., and Stouthamer, A. H. (1990) Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation, FEBS Lett. 275, 217-220.
    • (1990) FEBS Lett. , vol.275 , pp. 217-220
    • Van Spanning, R.J.1    Wansell, C.W.2    Reijnders, W.N.3    Oltmann, L.F.4    Stouthamer, A.H.5
  • 7
    • 0022400803 scopus 로고
    • An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role
    • Husain, M., and Davidson, V. L. (1985) An inducible periplasmic blue copper protein from Paracoccus denitrificans. Purification, properties, and physiological role, J. Biol. Chem. 260, 14626-14629.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14626-14629
    • Husain, M.1    Davidson, V.L.2
  • 8
    • 0038070331 scopus 로고    scopus 로고
    • MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis
    • Wang, Y., Graichen, M. E., Liu, A., Pearson, A. R., Wilmot, C. M., and Davidson, V. L. (2003) MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis, Biochemistry 42, 7318-7325.
    • (2003) Biochemistry , vol.42 , pp. 7318-7325
    • Wang, Y.1    Graichen, M.E.2    Liu, A.3    Pearson, A.R.4    Wilmot, C.M.5    Davidson, V.L.6
  • 9
    • 31044447260 scopus 로고    scopus 로고
    • Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis
    • Li, X., Feng, M., Wang, Y., Tachikawa, H., and Davidson, V. L. (2006) Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis, Biochemistry 45, 821-828.
    • (2006) Biochemistry , vol.45 , pp. 821-828
    • Li, X.1    Feng, M.2    Wang, Y.3    Tachikawa, H.4    Davidson, V.L.5
  • 11
    • 33749163547 scopus 로고    scopus 로고
    • Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase
    • Pearson, A. R., Marimanikkuppam, S., Li, X., Davidson, V. L., and Wilmot, C. M. (2006) Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase, J. Am. Chem. Soc. 128, 12416-12417.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12416-12417
    • Pearson, A.R.1    Marimanikkuppam, S.2    Li, X.3    Davidson, V.L.4    Wilmot, C.M.5
  • 12
    • 20444493512 scopus 로고    scopus 로고
    • MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase
    • Wang, Y., Li, X., Jones, L. H., Pearson, A. R., Wilmot, C. M., and Davidson, V. L. (2005) MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase, J. Am. Chem. Soc. 127, 8258-8259.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8258-8259
    • Wang, Y.1    Li, X.2    Jones, L.H.3    Pearson, A.R.4    Wilmot, C.M.5    Davidson, V.L.6
  • 13
    • 0032788792 scopus 로고    scopus 로고
    • Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides
    • Graichen, M. E., Jones, L. H., Sharma, B. V., van Spanning, R. J., Hosler, J. P., and Davidson, V. L. (1999) Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides, J. Bacteriol. 181, 4216-4222.
    • (1999) J. Bacteriol. , vol.181 , pp. 4216-4222
    • Graichen, M.E.1    Jones, L.H.2    Sharma, B.V.3    Van Spanning, R.J.4    Hosler, J.P.5    Davidson, V.L.6
  • 14
    • 0023668177 scopus 로고
    • Redox properties of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
    • Husain, M., Davidson, V. L., Gray, K. A., and Knaff, D. B. (1987) Redox properties of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans, Biochemistry 26, 4139-4143.
    • (1987) Biochemistry , vol.26 , pp. 4139-4143
    • Husain, M.1    Davidson, V.L.2    Gray, K.A.3    Knaff, D.B.4
  • 16
    • 26844501423 scopus 로고    scopus 로고
    • Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically
    • Lu, H., and Woodburn, J. (2005) Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically, J. Mol. Biol. 353, 897-910.
    • (2005) J. Mol. Biol. , vol.353 , pp. 897-910
    • Lu, H.1    Woodburn, J.2
  • 17
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • Aslund, F., Berndt, K. D., and Holmgren, A. (1997) Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria, J. Biol. Chem. 272, 30780-30786.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30780-30786
    • Aslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 18
    • 0023217278 scopus 로고
    • Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans
    • Husain, M., and Davidson, V. L. (1987) Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans, J. Bacteriol. 169, 1712-1717.
    • (1987) J. Bacteriol. , vol.169 , pp. 1712-1717
    • Husain, M.1    Davidson, V.L.2
  • 21
    • 0037040888 scopus 로고    scopus 로고
    • A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c
    • Ren, Q., Ahuja, U., and Thony-Meyer, L. (2002) A bacterial cytochrome c heme lyase. CcmF forms a complex with the heme chaperone CcmE and CcmH but not with apocytochrome c, J. Biol. Chem. 277, 7657-7663.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7657-7663
    • Ren, Q.1    Ahuja, U.2    Thony-Meyer, L.3
  • 22
    • 0034770083 scopus 로고    scopus 로고
    • Roles of thiol-redox pathways in bacteria
    • Ritz, D., and Beckwith, J. (2001) Roles of thiol-redox pathways in bacteria, Annu. Rev. Microbiol. 55, 21-48.
    • (2001) Annu. Rev. Microbiol. , vol.55 , pp. 21-48
    • Ritz, D.1    Beckwith, J.2
  • 23
    • 0023003367 scopus 로고
    • Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans
    • Gray, K. A., Knaff, D. B., Husain, M., and Davidson, V. L. (1986) Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans, FEBS Lett. 207, 239-242.
    • (1986) FEBS Lett. , vol.207 , pp. 239-242
    • Gray, K.A.1    Knaff, D.B.2    Husain, M.3    Davidson, V.L.4
  • 24
    • 0022998580 scopus 로고
    • Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans
    • Husain, M., and Davidson, V. L. (1986) Characterization of two inducible periplasmic c-type cytochromes from Paracoccus denitrificans, J. Biol. Chem. 261, 8577-8580.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8577-8580
    • Husain, M.1    Davidson, V.L.2
  • 25
    • 25444517605 scopus 로고    scopus 로고
    • A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm
    • Pittman, M. S., Robinson, H. C., and Poole, R. K. (2005) A bacterial glutathione transporter (Escherichia coli CydDC) exports reductant to the periplasm, J. Biol. Chem. 280, 32254-32261.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32254-32261
    • Pittman, M.S.1    Robinson, H.C.2    Poole, R.K.3
  • 26
    • 0242608621 scopus 로고    scopus 로고
    • Pathways of oxidative damage
    • Imlay, J. A. (2003) Pathways of oxidative damage, Annu. Rev. Microbiol. 57, 395-418.
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 395-418
    • Imlay, J.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.