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Volumn 108, Issue 1, 2011, Pages 97-102

Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization

Author keywords

Enzyme mechanism; Tetrapyrrole biosynthesis

Indexed keywords

BACTERIAL ENZYME; CBIK ENZYME; CBIX ENZYME; CHELATASE; CHLORINE; COLBALTOCHELATASE; FERROCHELATASE; LYASE; PROTOPORPHYRIN; SIROHYDROCHLORIN; UNCLASSIFIED DRUG;

EID: 78651075909     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1014298108     Document Type: Article
Times cited : (37)

References (37)
  • 1
    • 33644816286 scopus 로고    scopus 로고
    • Chelatases: Distort to select?
    • Al-Karadaghi S, et al. (2006) Chelatases: Distort to select? Trends Biochem Sci 31:135-142.
    • (2006) Trends Biochem Sci , vol.31 , pp. 135-142
    • Al-Karadaghi, S.1
  • 3
    • 0034486335 scopus 로고    scopus 로고
    • Ferrochelatase at the millennium: Structures, mechanisms and [2Fe-2S] clusters
    • Dailey HA, et al. (2000) Ferrochelatase at the millennium: Structures, mechanisms and [2Fe-2S] clusters. Cell Mol Life Sci 57:1909-1926.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1909-1926
    • Dailey, H.A.1
  • 5
    • 33747653529 scopus 로고    scopus 로고
    • S, from Archaeoglobus fulgidus
    • S, from Archaeoglobus fulgidus. J Struct Funct Genomics 7:37-50.
    • (2006) J Struct Funct Genomics , vol.7 , pp. 37-50
    • Yin, J.1
  • 6
    • 0033578347 scopus 로고    scopus 로고
    • Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis
    • Schubert HL, Raux E, Wilson KS, Warren MJ (1999) Common chelatase design in the branched tetrapyrrole pathways of heme and anaerobic cobalamin synthesis. Biochemistry 38:10660-10669.
    • (1999) Biochemistry , vol.38 , pp. 10660-10669
    • Schubert, H.L.1    Raux, E.2    Wilson, K.S.3    Warren, M.J.4
  • 7
    • 0031573454 scopus 로고    scopus 로고
    • Crystal structure of ferrochelatase: The terminal enzyme in heme biosynthesis
    • Al-Karadaghi S, Hansson M, Nikonov S, Jonsson B, Hedersted L (1997) Crystal structure of ferrochelatase: The terminal enzyme in heme biosynthesis. Structure 5:1501-1510.
    • (1997) Structure , vol.5 , pp. 1501-1510
    • Al-Karadaghi, S.1    Hansson, M.2    Nikonov, S.3    Jonsson, B.4    Hedersted, L.5
  • 8
    • 0142149159 scopus 로고    scopus 로고
    • L: Evidence for a 4Fe-4S center housed within an MXCXXC motif
    • L: Evidence for a 4Fe-4S center housed within an MXCXXC motif. J Biol Chem 278:41900-41907.
    • (2003) J Biol Chem , vol.278 , pp. 41900-41907
    • Leech, H.K.1
  • 9
    • 0037337451 scopus 로고    scopus 로고
    • Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin Bacillus megaterium
    • Raux E, et al. (2003) Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin Bacillus megaterium. Biochem J 370:505-516.
    • (2003) Biochem J , vol.370 , pp. 505-516
    • Raux, E.1
  • 10
    • 0033760278 scopus 로고    scopus 로고
    • Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis
    • Dashper SG, et al. (2000) Characterization of a novel outer membrane hemin-binding protein of Porphyromonas gingivalis. J Bacteriol 182:6456-6462.
    • (2000) J Bacteriol , vol.182 , pp. 6456-6462
    • Dashper, S.G.1
  • 11
    • 0033749406 scopus 로고    scopus 로고
    • Identification of an antigenic protein Pga30 from Porphyromonas gingivalis W50
    • Hendtlass A, Dashper SG, Reynolds EC (2000) Identification of an antigenic protein Pga30 from Porphyromonas gingivalis W50. Oral Microbiol Immun 15:383-387.
    • (2000) Oral Microbiol Immun , vol.15 , pp. 383-387
    • Hendtlass, A.1    Dashper, S.G.2    Reynolds, E.C.3
  • 12
    • 0034704158 scopus 로고    scopus 로고
    • 12) biosynthesis in Porphyromonas gingivalis. Identification and characterization of a functional corrin pathway
    • 12) biosynthesis in Porphyromonas gingivalis. Identification and characterization of a functional corrin pathway. J Biol Chem 275:40316-40323.
    • (2000) J Biol Chem , vol.275 , pp. 40316-40323
    • Roper, J.M.1
  • 13
    • 44349097016 scopus 로고    scopus 로고
    • Two distinct roles for two functional cobaltochelatases (CbiK) in Desulfovibrio vulgaris hildenborough
    • Lobo SA, et al. (2008) Two distinct roles for two functional cobaltochelatases (CbiK) in Desulfovibrio vulgaris hildenborough. Biochemistry 47:5851-5857.
    • (2008) Biochemistry , vol.47 , pp. 5851-5857
    • Lobo, S.A.1
  • 14
    • 0021100163 scopus 로고
    • Bovine ferrochelatase. Kinetic analysis of inhibition by N-methylprotoporphyrin, manganese, and heme
    • Dailey HA, Fleming JE (1983) Bovine ferrochelatase. Kinetic analysis of inhibition by N-methylprotoporphyrin, manganese, and heme. J Biol Chem 258:11453-11459.
    • (1983) J Biol Chem , vol.258 , pp. 11453-11459
    • Dailey, H.A.1    Fleming, J.E.2
  • 15
    • 0034677673 scopus 로고    scopus 로고
    • Structural and mechanistic basis of porphyrin metallation by ferrochelatase
    • Lecerof D, Fodje M, Hansson A, Hansson M, Al-Karadaghi S (2000) Structural and mechanistic basis of porphyrin metallation by ferrochelatase. J Mol Biol 297:221-232.
    • (2000) J Mol Biol , vol.297 , pp. 221-232
    • Lecerof, D.1    Fodje, M.2    Hansson, A.3    Hansson, M.4    Al-Karadaghi, S.5
  • 17
    • 0032514647 scopus 로고    scopus 로고
    • Structural and kinetic evidence for strain in biological catalysis
    • Romesberg FE, et al. (1998) Structural and kinetic evidence for strain in biological catalysis. Biochemistry 37:14404-14409.
    • (1998) Biochemistry , vol.37 , pp. 14404-14409
    • Romesberg, F.E.1
  • 18
    • 42649101624 scopus 로고    scopus 로고
    • Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: The role of active site residues
    • Karlberg T, et al. (2008) Porphyrin binding and distortion and substrate specificity in the ferrochelatase reaction: The role of active site residues. J Mol Biol 378:1074-1083.
    • (2008) J Mol Biol , vol.378 , pp. 1074-1083
    • Karlberg, T.1
  • 20
    • 0034746571 scopus 로고    scopus 로고
    • The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis
    • Wu CK, et al. (2001) The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat Struct Biol 8:156-160.
    • (2001) Nat Struct Biol , vol.8 , pp. 156-160
    • Wu, C.K.1
  • 21
    • 0037137256 scopus 로고    scopus 로고
    • Metal binding to Saccharomyces cerevisiae ferrochelatase
    • Karlberg T, et al. (2002) Metal binding to Saccharomyces cerevisiae ferrochelatase. Biochemistry 41:13499-13506.
    • (2002) Biochemistry , vol.41 , pp. 13499-13506
    • Karlberg, T.1
  • 22
    • 33846067247 scopus 로고    scopus 로고
    • Amino acid residues His183 and Glu264 in Bacillus subtilisferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX
    • Hansson MD, Karlberg T, Rahardja MA, Al-Karadaghi S, Hansson M (2007) Amino acid residues His183 and Glu264 in Bacillus subtilisferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX. Biochemistry 46:87-94.
    • (2007) Biochemistry , vol.46 , pp. 87-94
    • Hansson, M.D.1    Karlberg, T.2    Rahardja, M.A.3    Al-Karadaghi, S.4    Hansson, M.5
  • 23
    • 0035928770 scopus 로고    scopus 로고
    • Human ferrochelatase: Characterization of substrate-iron binding and proton-abstracting residues
    • Sellers VM, Wu CK, Dailey TA, Dailey HA (2001) Human ferrochelatase: Characterization of substrate-iron binding and proton-abstracting residues. Biochemistry 40:9821-9827.
    • (2001) Biochemistry , vol.40 , pp. 9821-9827
    • Sellers, V.M.1    Wu, C.K.2    Dailey, T.A.3    Dailey, H.A.4
  • 24
    • 22244450719 scopus 로고    scopus 로고
    • Protein families and their evolution-a structural perspective
    • Orengo CA, Thornton JM (2005) Protein families and their evolution-a structural perspective. Annu Rev Biochem 74:867-900.
    • (2005) Annu Rev Biochem , vol.74 , pp. 867-900
    • Orengo, C.A.1    Thornton, J.M.2
  • 25
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16:566-567.
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 26
    • 14844323140 scopus 로고    scopus 로고
    • Reaction mechanism of porphyrin metallation studied by theoretical methods
    • Shen Y, Ryde U (2005) Reaction mechanism of porphyrin metallation studied by theoretical methods. Chemistry 11:1549-1564.
    • (2005) Chemistry , vol.11 , pp. 1549-1564
    • Shen, Y.1    Ryde, U.2
  • 27
    • 34848852657 scopus 로고    scopus 로고
    • A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase
    • Medlock AE, Dailey TA, Ross TA, Dailey HA, Lanzilotta WN (2007) A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase. J Mol Biol 373:1006-1016.
    • (2007) J Mol Biol , vol.373 , pp. 1006-1016
    • Medlock, A.E.1    Dailey, T.A.2    Ross, T.A.3    Dailey, H.A.4    Lanzilotta, W.N.5
  • 28
    • 0035121475 scopus 로고    scopus 로고
    • CHOOCH: A program for deriving anomalous-scattering factors from X-ray fluorescence spectra
    • Evans G, Pettifer RF (2001) CHOOCH: A program for deriving anomalous-scattering factors from X-ray fluorescence spectra. J Appl Crystallogr 34:82-86.
    • (2001) J Appl Crystallogr , vol.34 , pp. 82-86
    • Evans, G.1    Pettifer, R.F.2
  • 29
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W (1993) Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800.
    • (1993) J Appl Crystallogr , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 30
    • 0030841590 scopus 로고    scopus 로고
    • Collaborative Computational Project Number 4: Providing programs for protein crystallography
    • Dodson EJ, Winn M, Ralph A (1997) Collaborative Computational Project Number 4: Providing programs for protein crystallography. Methods Enzymol 277:620-633.
    • (1997) Methods Enzymol , vol.277 , pp. 620-633
    • Dodson, E.J.1    Winn, M.2    Ralph, A.3
  • 31
    • 0013054388 scopus 로고    scopus 로고
    • Macromolecular phasing with SHELXE
    • Sheldrick GM (2002) Macromolecular phasing with SHELXE. Z Kristallogr 217:644-650.
    • (2002) Z Kristallogr , vol.217 , pp. 644-650
    • Sheldrick, G.M.1
  • 32
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A, Morris R, Lamzin VS (1999) Automated protein model building combined with iterative structure refinement. Nat Struct Biol 6:458-463.
    • (1999) Nat Struct Biol , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 34
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin A, Teplyakov A (1997) MOLREP: An automated program for molecular replacement. J Applied Crystallogr 30:1022-1025.
    • (1997) J Applied Crystallogr , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 35
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53:240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 36
    • 13244281317 scopus 로고    scopus 로고
    • COOT: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) COOT: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 37
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D 60:2256-2268.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.