메뉴 건너뛰기




Volumn 276, Issue 16, 2009, Pages 4414-4425

The effect of pH on the initial rate kinetics of the dimeric biliverdin-IXα reductase from the cyanobacterium Synechocystis PCC6803

Author keywords

Biliverdin reductase; Compulsory ordered mechanism; Dimer; PH; Synechocystis

Indexed keywords

BACTERIAL ENZYME; BILIVERDIN; BILIVERDIN IX ALPHA REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG;

EID: 68749083803     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07149.x     Document Type: Article
Times cited : (9)

References (36)
  • 1
  • 2
    • 0032503986 scopus 로고    scopus 로고
    • Primary production of the biosphere: Integrating terrestrial and oceanic components
    • Field CB, Behrenfeld MJ, Randerson JT Falkowski P (1998) Primary production of the biosphere: integrating terrestrial and oceanic components. Science 281, 237 240.
    • (1998) Science , vol.281 , pp. 237-240
    • Field, C.B.1    Behrenfeld, M.J.2    Randerson, J.T.3    Falkowski, P.4
  • 3
    • 0033009854 scopus 로고    scopus 로고
    • Prochlorococcus, a marine photosynthetic prokaryote of global significance
    • Partensky F, Hess WR Vaulot D (1999) Prochlorococcus, a marine photosynthetic prokaryote of global significance. Microbiol Mol Biol Rev 63, 106 127.
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 106-127
    • Partensky, F.1    Hess, W.R.2    Vaulot, D.3
  • 4
    • 0035032642 scopus 로고    scopus 로고
    • Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms
    • Frankenberg N, Mukougawa K, Kohchi T Lagarias JC (2001) Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms. Plant Cell 13, 965 978.
    • (2001) Plant Cell , vol.13 , pp. 965-978
    • Frankenberg, N.1    Mukougawa, K.2    Kohchi, T.3    Lagarias, J.C.4
  • 5
    • 0030925429 scopus 로고    scopus 로고
    • Characterization of cyanobacterial biliverdin reductase. Conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis
    • Schluchter WM Glazer AN (1997) Characterization of cyanobacterial biliverdin reductase. Conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis. J Biol Chem 272, 13562 13569.
    • (1997) J Biol Chem , vol.272 , pp. 13562-13569
    • Schluchter, W.M.1    Glazer, A.N.2
  • 9
    • 0035126828 scopus 로고    scopus 로고
    • Turning green to gold
    • McDonagh AF (2001) Turning green to gold. Nat Struct Biol 8, 198 200.
    • (2001) Nat Struct Biol , vol.8 , pp. 198-200
    • McDonagh, A.F.1
  • 11
    • 0036304792 scopus 로고    scopus 로고
    • Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex
    • Whitby FG, Phillips JD, Hill CP, McCoubrey W Maines MD (2002) Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex. J Mol Biol 319, 1199 1210.
    • (2002) J Mol Biol , vol.319 , pp. 1199-1210
    • Whitby, F.G.1    Phillips, J.D.2    Hill, C.P.3    McCoubrey, W.4    Maines, M.D.5
  • 13
    • 0029014160 scopus 로고
    • Purification and properties of salmon liver biliverdin reductase
    • Elliott G Mantle TJ (1995) Purification and properties of salmon liver biliverdin reductase. Biochem Soc Trans 23, 389S.
    • (1995) Biochem Soc Trans , vol.23
    • Elliott, G.1    Mantle, T.J.2
  • 15
    • 0018532963 scopus 로고
    • Purification and properties of biliverdin reductases from pig spleen and rat liver
    • Noguchi M, Yoshida T Kikuchi G (1979) Purification and properties of biliverdin reductases from pig spleen and rat liver. J Biochem 86, 833 848.
    • (1979) J Biochem , vol.86 , pp. 833-848
    • Noguchi, M.1    Yoshida, T.2    Kikuchi, G.3
  • 16
    • 0027199553 scopus 로고
    • Purification and characterization of human biliverdin reductase
    • Maines MD Trakshel GM (1993) Purification and characterization of human biliverdin reductase. Arch Biochem Biophys 300, 320 326.
    • (1993) Arch Biochem Biophys , vol.300 , pp. 320-326
    • Maines, M.D.1    Trakshel, G.M.2
  • 17
    • 0019598530 scopus 로고
    • Some kinetic and physical properties of biliverdin reductase
    • Phillips O Mantle TJ (1981) Some kinetic and physical properties of biliverdin reductase. Biochem Soc Trans 9, 275 278.
    • (1981) Biochem Soc Trans , vol.9 , pp. 275-278
    • Phillips, O.1    Mantle, T.J.2
  • 18
    • 0008886404 scopus 로고
    • Graphical determination of the dissociation constants for two-substrate enzyme systems
    • Florini JR Vestling CS (1957) Graphical determination of the dissociation constants for two-substrate enzyme systems. Biochim Biophys Acta 25, 575 578.
    • (1957) Biochim Biophys Acta , vol.25 , pp. 575-578
    • Florini, J.R.1    Vestling, C.S.2
  • 19
    • 0026480911 scopus 로고
    • Conformation inversion of bilirubin formed by reduction of the biliverdin-human serum albumin complex: Evidence from circular dichroism
    • Trull FR, Ibars O Lightner DA (1992) Conformation inversion of bilirubin formed by reduction of the biliverdin-human serum albumin complex: evidence from circular dichroism. Arch Biochem Biophys 298, 710 714.
    • (1992) Arch Biochem Biophys , vol.298 , pp. 710-714
    • Trull, F.R.1    Ibars, O.2    Lightner, D.A.3
  • 20
    • 0030670296 scopus 로고    scopus 로고
    • Cloning and overexpression of rat kidney biliverdin IX alpha reductase as a fusion protein with glutathione S-transferase: Stereochemistry of NADH oxidation and evidence that the presence of the glutathione S-transferase domain does not effect BVR-A activity
    • Ennis O, Maytum R Mantle TJ (1997) Cloning and overexpression of rat kidney biliverdin IX alpha reductase as a fusion protein with glutathione S-transferase: stereochemistry of NADH oxidation and evidence that the presence of the glutathione S-transferase domain does not effect BVR-A activity. Biochem J 328, 33 36.
    • (1997) Biochem J , vol.328 , pp. 33-36
    • Ennis, O.1    Maytum, R.2    Mantle, T.J.3
  • 22
    • 0034624024 scopus 로고    scopus 로고
    • Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation
    • Lott JS, Halbig D, Baker HM, Hardman MJ, Sprenger GA Baker EN (2000) Crystal structure of a truncated mutant of glucose-fructose oxidoreductase shows that an N-terminal arm controls tetramer formation. J Mol Biol 304, 575 584.
    • (2000) J Mol Biol , vol.304 , pp. 575-584
    • Lott, J.S.1    Halbig, D.2    Baker, H.M.3    Hardman, M.J.4    Sprenger, G.A.5    Baker, E.N.6
  • 23
    • 0034705454 scopus 로고    scopus 로고
    • Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. Structure-activity relationships define models for both active sites
    • Cunningham O, Dunne A, Sabido P, Lightner D Mantle TJ (2000) Studies on the specificity of the tetrapyrrole substrate for human biliverdin-IXalpha reductase and biliverdin-IXbeta reductase. Structure-activity relationships define models for both active sites. J Biol Chem 275, 19009 19017.
    • (2000) J Biol Chem , vol.275 , pp. 19009-19017
    • Cunningham, O.1    Dunne, A.2    Sabido, P.3    Lightner, D.4    Mantle, T.J.5
  • 25
    • 42449101715 scopus 로고    scopus 로고
    • Computational and experimental studies on the catalytic mechanism of biliverdin-IXbeta reductase
    • Smith LJ, Browne S, Mulholland AJ Mantle TJ (2008) Computational and experimental studies on the catalytic mechanism of biliverdin-IXbeta reductase. Biochem J 411, 475 484.
    • (2008) Biochem J , vol.411 , pp. 475-484
    • Smith, L.J.1    Browne, S.2    Mulholland, A.J.3    Mantle, T.J.4
  • 26
    • 56749163372 scopus 로고    scopus 로고
    • Stereoselective bile pigment binding to polypeptides and albumins: A circular dichroism study
    • Goncharova I Urbanová M (2008) Stereoselective bile pigment binding to polypeptides and albumins: a circular dichroism study. Anal Bioanal Chem 392, 1355 1365.
    • (2008) Anal Bioanal Chem , vol.392 , pp. 1355-1365
    • Goncharova, I.1    Urbanová, M.2
  • 27
    • 0030963706 scopus 로고    scopus 로고
    • Exciton chirality of bilirubin homologs
    • Boiadjiev SE Lightner DA (1997) Exciton chirality of bilirubin homologs. Chirality 9, 604 615.
    • (1997) Chirality , vol.9 , pp. 604-615
    • Boiadjiev, S.E.1    Lightner, D.A.2
  • 28
    • 0028958953 scopus 로고
    • Structure determination of the biliverdin apomyoglobin complex: Crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution
    • Wagner UG, Müller N, Schmitzberger W, Falk H Kratky C (1995) Structure determination of the biliverdin apomyoglobin complex: crystal structure analysis of two crystal forms at 1.4 and 1.5 A resolution. J Mol Biol 247, 326 337.
    • (1995) J Mol Biol , vol.247 , pp. 326-337
    • Wagner, U.G.1    Müller, N.2    Schmitzberger, W.3    Falk, H.4    Kratky, C.5
  • 29
    • 47049119049 scopus 로고    scopus 로고
    • Crystallographic analysis of human serum albumin complexed with 4Z,15E-bilirubin-IXalpha
    • Zunszain PA, Ghuman J, McDonagh AF Curry S (2008) Crystallographic analysis of human serum albumin complexed with 4Z,15E-bilirubin-IXalpha. J Mol Biol 381, 394 406.
    • (2008) J Mol Biol , vol.381 , pp. 394-406
    • Zunszain, P.A.1    Ghuman, J.2    McDonagh, A.F.3    Curry, S.4
  • 32
    • 33748754247 scopus 로고    scopus 로고
    • Insights into phycoerythrobilin biosynthesis point toward metabolic channeling
    • Dammeyer T Frankenberg-Dinkel N (2006) Insights into phycoerythrobilin biosynthesis point toward metabolic channeling. J Biol Chem 281, 27081 27089.
    • (2006) J Biol Chem , vol.281 , pp. 27081-27089
    • Dammeyer, T.1    Frankenberg-Dinkel, N.2
  • 33
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • In. Harding, S.E. Rowe, A.J. Horton, J.C. eds), pp. Royal Society of Chemistry. Cambridge.
    • Laue T, Shah B, Ridgeway T Pelletier S (1992) Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science (Harding SE, Rowe AJ Horton JC, eds), pp 90 125. Royal Society of Chemistry, Cambridge.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.1    Shah, B.2    Ridgeway, T.3    Pelletier, S.4
  • 34
    • 0343471377 scopus 로고    scopus 로고
    • Modification of a PCR-based site-directed mutagenesis method
    • Fisher CL Pei GK (1997) Modification of a PCR-based site-directed mutagenesis method. BioTechniques 23, 570 571.
    • (1997) BioTechniques , vol.23 , pp. 570-571
    • Fisher, C.L.1    Pei, G.K.2
  • 35
    • 0020629405 scopus 로고
    • The effect of pH on the kinetics of arylsulphatases A and B
    • O'Fagain C, Butler BM Mantle TJ (1983) The effect of pH on the kinetics of arylsulphatases A and B. Biochem J 213, 603 607.
    • (1983) Biochem J , vol.213 , pp. 603-607
    • O'Fagain, C.1    Butler, B.M.2    Mantle, T.J.3
  • 36
    • 0027249687 scopus 로고
    • Inactivation of mouse liver glutathione S-transferase YfYf (Pi class) by ethacrynic acid and 5,5′-dithiobis-(2-nitrobenzoic acid)
    • Phillips MF Mantle TJ (1993) Inactivation of mouse liver glutathione S-transferase YfYf (Pi class) by ethacrynic acid and 5,5′-dithiobis-(2- nitrobenzoic acid). Biochem J 294, 57 62.
    • (1993) Biochem J , vol.294 , pp. 57-62
    • Phillips, M.F.1    Mantle, T.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.