메뉴 건너뛰기




Volumn 50, Issue 9, 2011, Pages 1556-1566

Characterization of a protein-generated O 2 binding pocket in PqqC, a cofactorless oxidase catalyzing the final step in PQQ production

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING POCKETS; COFACTORS; ELECTRON ACCEPTOR; ENZYME ACTIVE SITES; GLUCOSE DEHYDROGENASE; OXIDATIVE CHEMISTRY; OXYGEN BINDING; RATE INCREASE; SPECTROPHOTOMETRIC ASSAYS;

EID: 79952123264     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1015474     Document Type: Article
Times cited : (13)

References (41)
  • 1
    • 0035212690 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes
    • Anthony, C. (2001) Pyrroloquinoline quinone (PQQ) and quinoprotein enzymes Antioxid. Redox Signaling 3, 757-774 (Pubitemid 33131268)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.5 , pp. 757-774
    • Anthony, C.1
  • 2
    • 14144253677 scopus 로고    scopus 로고
    • Cyclization mechanism for the synthesis of macrocyclic antibiotic lankacidin in Streptomyces rochei
    • DOI 10.1016/j.chembiol.2005.01.009
    • Arakawa, K., Sugino, F., Kodama, K., Ishii, T., and Kinashi, H. (2005) Cyclization mechanism for the synthesis of macrocyclic antibiotic lankacidin in Streptomyces rochei Chem. Biol. 12, 249-256 (Pubitemid 40281332)
    • (2005) Chemistry and Biology , vol.12 , Issue.2 , pp. 249-256
    • Arakawa, K.1    Sugino, F.2    Kodama, K.3    Ishii, T.4    Kinashi, H.5
  • 3
    • 0031733482 scopus 로고    scopus 로고
    • The biochemistry, physiology and genetics of PQQ and PQQ-containing enzymes
    • Goodwin, P. M. and Anthony, C. (1998) The biochemistry, physiology and genetics of PQQ and PQQ-containing enzymes Adv. Microb. Physiol. 40, 1-80 (Pubitemid 28537738)
    • (1998) Advances in Microbial Physiology , vol.40 , pp. 1-80
    • Goodwin, P.M.1    Anthony, C.2
  • 4
    • 3042691747 scopus 로고    scopus 로고
    • The quinoprotein dehydrogenases for methanol and glucose
    • DOI 10.1016/j.abb.2004.03.038, PII S0003986104001808
    • Anthony, C. (2004) The quinoprotein dehydrogenases for methanol and glucose Arch. Biochem. Biophys. 428, 2-9 (Pubitemid 38844904)
    • (2004) Archives of Biochemistry and Biophysics , vol.428 , Issue.1 , pp. 2-9
    • Anthony, C.1
  • 5
    • 79952127548 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone: Role in growth and development
    • Abstract 439.9.
    • Storms, D. H., Rucker, R. B., Chen, I. L. F., Jame, M., and Yang, S. J. (2003) Pyrroloquinoline quinone: role in growth and development. FASEB J. 17, Abstract 439.9.
    • (2003) FASEB J. , vol.17
    • Storms, D.H.1    Rucker, R.B.2    Chen, I.L.F.3    Jame, M.4    Yang, S.J.5
  • 7
    • 0037212893 scopus 로고    scopus 로고
    • Antioxidant and pro-oxidant properties of pyrroloquinoline quinone (PQQ): Implications for its function in biological systems
    • DOI 10.1016/S0006-2952(02)01453-3, PII S0006295202014533
    • He, K., Nukada, H., Urakami, T., and Murphy, M. P. (2003) Antioxidant and pro-oxidant properties of pyrroloquinoline quinone (PQQ): implications for its function in biological systems Biochem. Pharmacol. 65, 67-74 (Pubitemid 35447840)
    • (2003) Biochemical Pharmacology , vol.65 , Issue.1 , pp. 67-74
    • He, K.1    Nukada, H.2    Urakami, T.3    Murphy, M.P.4
  • 8
    • 0037465763 scopus 로고    scopus 로고
    • Understanding quinone cofactor biogenesis in methylamine dehydrogenase through novel cofactor generation
    • DOI 10.1021/bi027073a
    • Pearson, A. R., Jones, L. H., Higgins, L. A., Ashcroft, A. E., Wilmot, C. M., and Davidson, V. L. (2003) Understanding quinone cofactor biogenesis in methylamine dehydrogenase through novel cofactor generation Biochemistry 42, 3224-3230 (Pubitemid 36348630)
    • (2003) Biochemistry , vol.42 , Issue.11 , pp. 3224-3230
    • Pearson, A.R.1    Jones, L.H.2    Higgins, L.3    Ashcroft, A.E.4    Wilmot, C.M.5    Davidson, V.L.6
  • 9
    • 9744222639 scopus 로고    scopus 로고
    • Mechanism of post-translational quinone formation in copper amine oxidases and its relationship to the catalytic turnover
    • DOI 10.1016/j.abb.2004.08.036, PII S0003986104005223
    • DuBois, J. L. and Klinman, J. P. (2005) Mechanism of post-translational quinone formation in copper amine oxidases and its relationship to the catalytic turnover Arch. Biochem. Biophys. 433, 255-265 (Pubitemid 39586596)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 255-265
    • DuBois, J.L.1    Klinman, J.P.2
  • 10
    • 0031049495 scopus 로고    scopus 로고
    • Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate
    • Toyama, H., Chistoserdova, L., and Lidstrom, M. E. (1997) Sequence analysis of pqq genes required for biosynthesis of pyrroloquinoline quinone in Methylobacterium extorquens AM1 and the purification of a biosynthetic intermediate Microbiology 143, 595-602 (Pubitemid 27092198)
    • (1997) Microbiology , vol.143 , Issue.2 , pp. 595-602
    • Toyama, H.1    Chistoserdova, L.2    Lidstrom, M.E.3
  • 11
    • 0000521261 scopus 로고
    • Biosynthesis of pyrroloquinoline quinone. 2. Biosynthetic assembly from glutamate and tyrosine
    • Houck, D. R., Hanners, J. L., and Unkefer, C. J. (1991) Biosynthesis of pyrroloquinoline quinone. 2. Biosynthetic assembly from glutamate and tyrosine J. Am. Chem. Soc. 113, 3162-3166
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 3162-3166
    • Houck, D.R.1    Hanners, J.L.2    Unkefer, C.J.3
  • 13
    • 2342652839 scopus 로고    scopus 로고
    • The Structure of a Biosynthetic Intermediate of Pyrroloquinoline Quinone (PQQ) and Elucidation of the Final Step of PQQ Biosynthesis
    • DOI 10.1021/ja0493852
    • Magnusson, O. T., Toyama, H., Saeki, M., Schwarzenbacher, R., and Klinman, J. P. (2004) The structure of a biosynthetic intermediate of pyrroloquinoline quinone (PQQ) and elucidation of the final step of PQQ biosynthesis J. Am. Chem. Soc. 126, 5342-5343 (Pubitemid 38596330)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.17 , pp. 5342-5343
    • Magnusson, O.T.1    Toyama, H.2    Saeki, M.3    Schwarzenbacher, R.4    Klinman, J.P.5
  • 15
    • 34250850181 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone biogenesis: Characterization of PqqC and its H84N and H84A active site variants
    • DOI 10.1021/bi700162n
    • Magnusson, O. T., RoseFigura, J. M., Toyama, H., Schwarzenbacher, R., and Klinman, J. P. (2007) Pyrroloquinoline quinone biogenesis: characterization of PqqC and its H84N and H84A active site variants Biochemistry 46, 7174-7186 (Pubitemid 46973991)
    • (2007) Biochemistry , vol.46 , Issue.24 , pp. 7174-7186
    • Magnusson, O.Th.1    Rosefigura, J.M.2    Toyama, H.3    Schwarzenbacher, R.4    Klinman, J.P.5
  • 18
    • 0026549104 scopus 로고
    • Nucleotide-sequencing and structure of the Klebsiella pneumoniae PQQ operon
    • Meulenberg, J. J. M., Sellink, E., Riegman, N. H., and Postma, P. W. (1992) Nucleotide-sequencing and structure of the Klebsiella pneumoniae PQQ operon Mol. Gen. Genet. 232, 284-294
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 284-294
    • Meulenberg, J.J.M.1    Sellink, E.2    Riegman, N.H.3    Postma, P.W.4
  • 20
    • 0030478428 scopus 로고    scopus 로고
    • Production, characterization, and reconstitution of recombinant quinoprotein glucose dehydrogenase (soluble type; EC 1.1.99.17) apoenzyme of Acinetobacter calcoaceticus
    • DOI 10.1006/abbi.1996.0530
    • Olsthoorn, A. J. J. and Duine, J. A. (1996) Production, characterization, and reconstitution of recombinant quinoprotein glucose dehydrogenase (soluble type; EC 1.1.99.17) apoenzyme of Acinetobacter calcoaceticus Arch. Biochem. Biophys. 336, 42-48 (Pubitemid 26423748)
    • (1996) Archives of Biochemistry and Biophysics , vol.336 , Issue.1 , pp. 42-48
    • Olsthoorn, A.J.J.1    Duine, J.A.2
  • 21
    • 33645986934 scopus 로고
    • Circular dichroism of quinoid pigments from Far Eastern representatives of the family Boraginaceae
    • Nabiullin, A. A., Fedoreev, S. A., and Deshko, T. N. (1984) Circular dichroism of quinoid pigments from Far Eastern representatives of the family Boraginaceae Chem. Nat. Compd. 19, 532-537
    • (1984) Chem. Nat. Compd. , vol.19 , pp. 532-537
    • Nabiullin, A.A.1    Fedoreev, S.A.2    Deshko, T.N.3
  • 25
    • 34447638717 scopus 로고    scopus 로고
    • How do enzymes activate oxygen without inactivating themselves?
    • Klinman, J. P. (2007) How do enzymes activate oxygen without inactivating themselves? Acc. Chem. Res. 40, 325-333
    • (2007) Acc. Chem. Res. , vol.40 , pp. 325-333
    • Klinman, J.P.1
  • 26
    • 0035905357 scopus 로고    scopus 로고
    • Oxygen binding, activation, and reduction to water by copper proteins
    • DOI 10.1002/1521-3773(20011217)40:24<4570::AID-ANIE4570>3.0.CO;2-4
    • Solomon, E. I., Chen, P., Metz, M., Lee, S. K., and Palmer, A. E. (2001) Oxygen binding, activation, and reduction to water by copper proteins Angew. Chem., Int. Ed. 40, 4570-4590 (Pubitemid 34032186)
    • (2001) Angewandte Chemie - International Edition , vol.40 , Issue.24 , pp. 4570-4590
    • Solomon, E.I.1    Chen, P.2    Metz, M.3    Lee, S.-K.4    Palmer, A.E.5
  • 27
    • 0037137223 scopus 로고    scopus 로고
    • Binding of dioxygen to non-metal sites in proteins: Exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha
    • DOI 10.1021/bi0204591
    • Goto, Y. and Klinman, J. P. (2002) Binding of dioxygen to non-metal sites in proteins: exploration of the importance of binding site size versus hydrophobicity in the copper amine oxidase from Hansenula polymorpha Biochemistry 41, 13637-13643 (Pubitemid 35332700)
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13637-13643
    • Goto, Y.1    Klinman, J.P.2
  • 31
    • 58849130685 scopus 로고    scopus 로고
    • Kinetics and spectroscopic evidence that the Cu(I)-semiquinone intermediate reduces molecular oxygen in the oxidative half-reaction of Arthrobacter globiformis amine oxidase
    • Shepard, E. M., Okonski, K. M., and Dooley, D. M. (2008) Kinetics and spectroscopic evidence that the Cu(I)-semiquinone intermediate reduces molecular oxygen in the oxidative half-reaction of Arthrobacter globiformis amine oxidase Biochemistry 47, 13907-13920
    • (2008) Biochemistry , vol.47 , pp. 13907-13920
    • Shepard, E.M.1    Okonski, K.M.2    Dooley, D.M.3
  • 32
    • 0032497371 scopus 로고    scopus 로고
    • Probing the mechanism of proton coupled electron transfer to dioxygen: The oxidative half reaction of bovinre serum amine oxidase
    • Su, Q. and Klinman, J. P. (1998) Probing the mechanism of proton coupled electron transfer to dioxygen: the oxidative half reaction of bovinre serum amine oxidase Biochemistry 37, 12513-12524
    • (1998) Biochemistry , vol.37 , pp. 12513-12524
    • Su, Q.1    Klinman, J.P.2
  • 34
    • 70350063829 scopus 로고    scopus 로고
    • Factors that affect oxygen activation and coupling of the two redox cycles in the aromatization reaction catalyzed by NikD, an unusual amino acid oxidase
    • Kommoju, P. R., Bruckner, R. C., Ferreira, P., Carrell, C. J., Mathews, F. S., and Jorns, M. S. (2009) Factors that affect oxygen activation and coupling of the two redox cycles in the aromatization reaction catalyzed by NikD, an unusual amino acid oxidase Biochemistry 48, 9542-9555
    • (2009) Biochemistry , vol.48 , pp. 9542-9555
    • Kommoju, P.R.1    Bruckner, R.C.2    Ferreira, P.3    Carrell, C.J.4    Mathews, F.S.5    Jorns, M.S.6
  • 35
    • 77950407407 scopus 로고    scopus 로고
    • Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase
    • Finnegan, S., Agniswamy, J., Weber, I. T., and Gadda, G. (2010) Role of valine 464 in the flavin oxidation reaction catalyzed by choline oxidase Biochemistry 49, 2952-2961
    • (2010) Biochemistry , vol.49 , pp. 2952-2961
    • Finnegan, S.1    Agniswamy, J.2    Weber, I.T.3    Gadda, G.4
  • 36
    • 71449113304 scopus 로고    scopus 로고
    • Involvement of ionizable groups in catalysis of human liver glycolate oxidase
    • Pennati, A. and Gadda, G. (2009) Involvement of ionizable groups in catalysis of human liver glycolate oxidase J. Biol. Chem. 284, 31214-31222
    • (2009) J. Biol. Chem. , vol.284 , pp. 31214-31222
    • Pennati, A.1    Gadda, G.2
  • 37
    • 77950626884 scopus 로고    scopus 로고
    • Cofactor-independent oxidases and oxygenases
    • Fetzner, S. and Steiner, R. A. (2010) Cofactor-independent oxidases and oxygenases Appl. Microbiol. Biotechnol. 86, 791-804
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 791-804
    • Fetzner, S.1    Steiner, R.A.2
  • 38
    • 48349141173 scopus 로고    scopus 로고
    • Oxygen pressurized X-ray crystallography: Probing the dioxygen binding site in cofactorless urate oxidase and implications for its catalytic mechanism
    • Colloch, N., Gabison, L., Monard, G., Altarsha, M., Chiadmi, M., Marassio, G., Santos, J., El Hajji, M., Castro, B., Abraini, J. H., and Prange, T. (2008) Oxygen pressurized X-ray crystallography: probing the dioxygen binding site in cofactorless urate oxidase and implications for its catalytic mechanism Biophys. J. 95, 2415-2422
    • (2008) Biophys. J. , vol.95 , pp. 2415-2422
    • Colloch, N.1    Gabison, L.2    Monard, G.3    Altarsha, M.4    Chiadmi, M.5    Marassio, G.6    Santos, J.7    El Hajji, M.8    Castro, B.9    Abraini, J.H.10    Prange, T.11
  • 39
    • 0019436436 scopus 로고
    • Characteristics of the cofactor requirements for the superoxide- generating NADPH oxidase of human polymorphonuclear leukocytes
    • DOI 10.1021/bi00509a010
    • Light, D. R., Walsh, C., Ocallaghan, A. M., Goetzl, E. J., and Tauber, A. I. (1981) Characteristic of the cofactor requirements of the superoxide-generating NADPH oxidase of human polymorphonuclear leukocytes Biochemistry 20, 1468-1476 (Pubitemid 11127108)
    • (1981) Biochemistry , vol.20 , Issue.6 , pp. 1468-1476
    • Light, D.R.1    Walsh, C.2    O'Callaghan, A.M.3
  • 40
    • 0033985880 scopus 로고    scopus 로고
    • Whence topa? Models for the biogenesis of topa quinone in copper amine oxidases
    • DOI 10.1016/S1381-1177(99)00071-5, PII S1381117799000715
    • Williams, N. K. and Klinman, J. P. (2000) Whence topa? Models for the biogenesis of topa quinone in copper amine oxidases J. Mol. Catal. B: Enzym. 8, 95-101 (Pubitemid 30035393)
    • (2000) Journal of Molecular Catalysis - B Enzymatic , vol.8 , Issue.1-3 , pp. 95-101
    • Williams, N.K.1    Klinman, J.P.2
  • 41
    • 0034603777 scopus 로고    scopus 로고
    • Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast
    • DOI 10.1021/bi992225w
    • Dove, J. E., Schwartz, B., Williams, N. K., and Klinman, J. P. (2000) Investigation of spectroscopic intermediates during copper-binding and TPQ formation in wild-type and active-site mutants of a copper-containing amine oxidase from yeast Biochemistry 39, 3690-3698 (Pubitemid 30183850)
    • (2000) Biochemistry , vol.39 , Issue.13 , pp. 3690-3698
    • Dove, J.E.1    Schwartz, B.2    Williams, N.K.3    Klinman, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.