메뉴 건너뛰기




Volumn 1794, Issue 9, 2009, Pages 1288-1298

Structural organization of WrbA in apo- and holoprotein crystals

Author keywords

Diffraction resolution; Dimerization; Disulfide; Electrostatic potential surface; NAD(P)H:quinone oxidoreductase; Trichloroacetic acid; Twisted open sheet fold

Indexed keywords

ESCHERICHIA COLI PROTEIN; FLAVODOXIN; PROTEIN WRBA; UNCLASSIFIED DRUG;

EID: 69249216528     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.08.001     Document Type: Article
Times cited : (13)

References (63)
  • 1
    • 0028587317 scopus 로고
    • Six new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin
    • Grandori R., and Carey J. Six new candidate members of the alpha/beta twisted open-sheet family detected by sequence similarity to flavodoxin. Protein Sci. 3 (1994) 2185-2193
    • (1994) Protein Sci. , vol.3 , pp. 2185-2193
    • Grandori, R.1    Carey, J.2
  • 2
    • 33646590587 scopus 로고    scopus 로고
    • WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase
    • Patridge E.V., and Ferry J.G. WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase. J. Bacteriol. 188 (2006) 3498-3506
    • (2006) J. Bacteriol. , vol.188 , pp. 3498-3506
    • Patridge, E.V.1    Ferry, J.G.2
  • 4
    • 0002117840 scopus 로고
    • DT-Diaphorase: a historical review
    • Ernster L. DT-Diaphorase: a historical review. Chem. Scr. 27A (1987) 1-13
    • (1987) Chem. Scr. , vol.27 A , pp. 1-13
    • Ernster, L.1
  • 5
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction
    • Li R., Bianchet M.A., Talalay P., and Amzel L.M. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc. Natl. Acad. Sci. U. S. A. 92 (1995) 8846-8850
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 6
    • 28844492234 scopus 로고    scopus 로고
    • Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide
    • Gorman J., and Shapiro L. Crystal structures of the tryptophan repressor binding protein WrbA and complexes with flavin mononucleotide. Protein Sci. 14 (2005) 3004-3012
    • (2005) Protein Sci. , vol.14 , pp. 3004-3012
    • Gorman, J.1    Shapiro, L.2
  • 7
    • 37449004250 scopus 로고    scopus 로고
    • Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli
    • Andrade S.L., Patridge E.V., Ferry J.G., and Einsle O. Crystal structure of the NADH:quinone oxidoreductase WrbA from Escherichia coli. J. Bacteriol. 189 (2007) 9101-9107
    • (2007) J. Bacteriol. , vol.189 , pp. 9101-9107
    • Andrade, S.L.1    Patridge, E.V.2    Ferry, J.G.3    Einsle, O.4
  • 8
    • 0032516896 scopus 로고    scopus 로고
    • Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins
    • Grandori R., Khalifah P., Boice J.A., Fairman R., Giovanelli K., and Carey J. Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins. J. Biol. Chem. 273 (1998) 20960-20966
    • (1998) J. Biol. Chem. , vol.273 , pp. 20960-20966
    • Grandori, R.1    Khalifah, P.2    Boice, J.A.3    Fairman, R.4    Giovanelli, K.5    Carey, J.6
  • 9
    • 33846243823 scopus 로고    scopus 로고
    • Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA
    • Natalello A., Doglia S.M., Carey J., and Grandori R. Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA. Biochemistry 46 (2007) 543-553
    • (2007) Biochemistry , vol.46 , pp. 543-553
    • Natalello, A.1    Doglia, S.M.2    Carey, J.3    Grandori, R.4
  • 10
    • 34248581202 scopus 로고    scopus 로고
    • Stress-inducible flavodoxin from photosynthetic microorganisms. The mystery of flavodoxin loss from the plant genome
    • Zurbriggen M.D., Tognetti V.B., and Carillo N. Stress-inducible flavodoxin from photosynthetic microorganisms. The mystery of flavodoxin loss from the plant genome. IUBMB Life 59 (2007) 355-360
    • (2007) IUBMB Life , vol.59 , pp. 355-360
    • Zurbriggen, M.D.1    Tognetti, V.B.2    Carillo, N.3
  • 11
    • 33747488135 scopus 로고    scopus 로고
    • Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance
    • Tognetti V.B., Palatnik J.F., Fillat M.F., Melzer M., Hajirezaei M.R., Valle E.M., and Carrillo N. Functional replacement of ferredoxin by a cyanobacterial flavodoxin in tobacco confers broad-range stress tolerance. Plant Cell 18 (2006) 2035-2050
    • (2006) Plant Cell , vol.18 , pp. 2035-2050
    • Tognetti, V.B.1    Palatnik, J.F.2    Fillat, M.F.3    Melzer, M.4    Hajirezaei, M.R.5    Valle, E.M.6    Carrillo, N.7
  • 12
    • 0020064853 scopus 로고
    • Routes of flavodoxin and ferredoxin reduction in E. 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. Routes of flavodoxin and ferredoxin reduction in E. coli. CoA-acylating pyruvate:flavodoxin and NADPH:flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase. Eur. J. Biochem. 123 (1982) 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
  • 13
    • 21244464767 scopus 로고    scopus 로고
    • fldA is an essential gene required in the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis
    • Puan K.J., Wang H., Dairi T., Kuzuyama T., and Morita C.T. fldA is an essential gene required in the 2-C-methyl-D-erythritol 4-phosphate pathway for isoprenoid biosynthesis. FEBS Lett. 579 (2005) 3802-3806
    • (2005) FEBS Lett. , vol.579 , pp. 3802-3806
    • Puan, K.J.1    Wang, H.2    Dairi, T.3    Kuzuyama, T.4    Morita, C.T.5
  • 14
    • 34447327214 scopus 로고    scopus 로고
    • Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide
    • Wolfova J., Mesters J.R., Brynda J., Grandori R., Natalello A., Carey J., and Kuta Smatanova I. Crystallization and preliminary diffraction analysis of Escherichia coli WrbA in complex with its cofactor flavin mononucleotide. Acta Crystallogr. F 63 (2007) 571-575
    • (2007) Acta Crystallogr. F , vol.63 , pp. 571-575
    • Wolfova, J.1    Mesters, J.R.2    Brynda, J.3    Grandori, R.4    Natalello, A.5    Carey, J.6    Kuta Smatanova, I.7
  • 15
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 16
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AmoRe
    • Navaza J. Implementation of molecular replacement in AmoRe. Acta Crystallogr. D 57 (2001) 1367-1372
    • (2001) Acta Crystallogr. D , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 17
    • 0028103275 scopus 로고
    • Collaborative Computational Project No. 4, The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project No. 4, The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50 (1994) 760-763
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 18
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53 (1997) 240-255
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 19
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit - a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 20
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60 (2004) 2126-2132
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 22
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., and Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372 (2007) 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 3242879177 scopus 로고    scopus 로고
    • iMolTalk: an interactive, internet-based protein structure analysis server
    • Diemand A.V., and Scheib H. iMolTalk: an interactive, internet-based protein structure analysis server. Nucleic Acids Res. 32 (2004) W512-516
    • (2004) Nucleic Acids Res. , vol.32
    • Diemand, A.V.1    Scheib, H.2
  • 24
    • 0035012982 scopus 로고    scopus 로고
    • STRAP: editor for STRuctural Alignments of Proteins
    • Gille C., and Frömmel C. STRAP: editor for STRuctural Alignments of Proteins. Bioinformatics 17 (2001) 377-378
    • (2001) Bioinformatics , vol.17 , pp. 377-378
    • Gille, C.1    Frömmel, C.2
  • 26
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA - a self-parameterizing force field
    • Krieger E., Koraimann G., and Vriend G. Increasing the precision of comparative models with YASARA NOVA - a self-parameterizing force field. Proteins 47 (2002) 393-402
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 27
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang J., Cieplak P., and Kollman P.A. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?. J. Comput. Chem. 21 (2000) 1049-1074
    • (2000) J. Comput. Chem. , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 30
    • 51149210396 scopus 로고
    • Determination of absolute from relative X-ray intensity data
    • Wilson A.J.C. Determination of absolute from relative X-ray intensity data. Nature 150 (1942) 151-152
    • (1942) Nature , vol.150 , pp. 151-152
    • Wilson, A.J.C.1
  • 31
    • 0027299601 scopus 로고
    • A stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNA
    • Yang W.P., Ni L.Y., and Somerville R.L. A stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNA. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 5796-5800
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 5796-5800
    • Yang, W.P.1    Ni, L.Y.2    Somerville, R.L.3
  • 33
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J. Mol. Biol. 33 (1968) 491-497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 34
    • 0031439702 scopus 로고    scopus 로고
    • Analysis of temperature factor distribution in high-resolution protein structures
    • Parthasarathy S., and Murthy M.R. Analysis of temperature factor distribution in high-resolution protein structures. Protein Sci. 6 (1997) 2561-2567
    • (1997) Protein Sci. , vol.6 , pp. 2561-2567
    • Parthasarathy, S.1    Murthy, M.R.2
  • 35
    • 43649086695 scopus 로고    scopus 로고
    • Phosphate binding energy and catalysis by small and large molecules
    • Morrow J.R., Aymes T.L., and Richard J.P. Phosphate binding energy and catalysis by small and large molecules. Acc. Chem. Res. 41 (2008) 539-548
    • (2008) Acc. Chem. Res. , vol.41 , pp. 539-548
    • Morrow, J.R.1    Aymes, T.L.2    Richard, J.P.3
  • 38
    • 33646052947 scopus 로고    scopus 로고
    • Flavodoxins: sequence, folding, binding, function and beyond
    • Sancho J. Flavodoxins: sequence, folding, binding, function and beyond. Cell. Mol. Life Sci. 63 (2006) 855-864
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 855-864
    • Sancho, J.1
  • 39
    • 0029989460 scopus 로고    scopus 로고
    • Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin
    • Genzor C.G., Perales-Alcón A., Sancho J., and Romero A. Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin. Nat. Struct. Biol. 3 (1996) 329-332
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 329-332
    • Genzor, C.G.1    Perales-Alcón, A.2    Sancho, J.3    Romero, A.4
  • 40
    • 0030167588 scopus 로고    scopus 로고
    • Possible role of a short extra loop of the long-chain flavodoxin from Azotobacter chrooccum in electron transfer to nitrogenase: complete 1H, 15n< and 13C backbone assignments and secondary structure of the flavodoxin
    • Peelen S., Wijmenga S.S., Erbel P.J.A., Robson R.L., Eady R.R., and Vervoort J. Possible role of a short extra loop of the long-chain flavodoxin from Azotobacter chrooccum in electron transfer to nitrogenase: complete 1H, 15n< and 13C backbone assignments and secondary structure of the flavodoxin. Biomol. NMR 7 (1996) 315-330
    • (1996) Biomol. NMR , vol.7 , pp. 315-330
    • Peelen, S.1    Wijmenga, S.S.2    Erbel, P.J.A.3    Robson, R.L.4    Eady, R.R.5    Vervoort, J.6
  • 42
    • 0034191064 scopus 로고    scopus 로고
    • The stability of thermophilic proteins: a study based on comprehensive genome comparison
    • Das R., and Gerstein M. The stability of thermophilic proteins: a study based on comprehensive genome comparison. Funct. Integr. Genomics 1 (2000) 76-88
    • (2000) Funct. Integr. Genomics , vol.1 , pp. 76-88
    • Das, R.1    Gerstein, M.2
  • 43
    • 0021404923 scopus 로고
    • Polar lipids from the radiation resistant bacterium Deinococcus radiodurans: structural investigations on glucosaminyl and N-acetyl glucosaminyl lipids
    • Carbonneau M.A., Rebeyrotte N., and Rebeyrotte P. Polar lipids from the radiation resistant bacterium Deinococcus radiodurans: structural investigations on glucosaminyl and N-acetyl glucosaminyl lipids. Biochimie 66 (1984) 319-330
    • (1984) Biochimie , vol.66 , pp. 319-330
    • Carbonneau, M.A.1    Rebeyrotte, N.2    Rebeyrotte, P.3
  • 44
    • 0035102449 scopus 로고    scopus 로고
    • Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics
    • Makarova K.S., Aravind L., Wolf Y.I., Tatusov R.L., Minton K.W., Koonin E.V., and Daly M.J. Genome of the extremely radiation-resistant bacterium Deinococcus radiodurans viewed from the perspective of comparative genomics. Microbiol. Mol. Biol. Rev. 65 (2001) 44-79
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 44-79
    • Makarova, K.S.1    Aravind, L.2    Wolf, Y.I.3    Tatusov, R.L.4    Minton, K.W.5    Koonin, E.V.6    Daly, M.J.7
  • 45
    • 0036777641 scopus 로고    scopus 로고
    • Envelope disorder of Escherichia coli cells lacking phosphatidylglycerol
    • Suzuki M., Hara H., and Matsumoto K. Envelope disorder of Escherichia coli cells lacking phosphatidylglycerol. J. Bacteriol. 184 (2002) 5418-5425
    • (2002) J. Bacteriol. , vol.184 , pp. 5418-5425
    • Suzuki, M.1    Hara, H.2    Matsumoto, K.3
  • 46
    • 0024601564 scopus 로고
    • Mechanisms of flavoprotein-catalyzed reactions
    • Ghisla S., and Massey V. Mechanisms of flavoprotein-catalyzed reactions. Eur. J. Biochem. 181 (1989) 1-17
    • (1989) Eur. J. Biochem. , vol.181 , pp. 1-17
    • Ghisla, S.1    Massey, V.2
  • 47
    • 33644881630 scopus 로고    scopus 로고
    • Spectroelectrochemical investigation of a flavoprotein with a flavin-modified gold electrode
    • Nöll G., Kozma E., Grandori R., Carey J., Schodl T., Hauska G., and Daub J. Spectroelectrochemical investigation of a flavoprotein with a flavin-modified gold electrode. Langmuir 22 (2006) 2378-2383
    • (2006) Langmuir , vol.22 , pp. 2378-2383
    • Nöll, G.1    Kozma, E.2    Grandori, R.3    Carey, J.4    Schodl, T.5    Hauska, G.6    Daub, J.7
  • 48
    • 0037474541 scopus 로고    scopus 로고
    • Structural characterisation and functional significance of transient protein-protein interactions
    • Nooren I.M.A., and Thornton J.M. Structural characterisation and functional significance of transient protein-protein interactions. J. Mol. Biol. 325 (2003) 991-1018
    • (2003) J. Mol. Biol. , vol.325 , pp. 991-1018
    • Nooren, I.M.A.1    Thornton, J.M.2
  • 49
    • 0242573143 scopus 로고    scopus 로고
    • Structure and function of photosystem I: interaction with its soluble electron carriers and external antenna systems
    • Fromme P., Melkozernov A., Jordan P., and Krauss N. Structure and function of photosystem I: interaction with its soluble electron carriers and external antenna systems. FEBS Lett. 555 (2003) 40-44
    • (2003) FEBS Lett. , vol.555 , pp. 40-44
    • Fromme, P.1    Melkozernov, A.2    Jordan, P.3    Krauss, N.4
  • 50
    • 0037465820 scopus 로고    scopus 로고
    • Structural analysis of the photosystem I supercomplex of cynaobacteria induced by iron deficiency
    • Nield J., Morris E.P., Bibby T.S., and Barber J. Structural analysis of the photosystem I supercomplex of cynaobacteria induced by iron deficiency. Biochemistry 42 (2003) 3180-3188
    • (2003) Biochemistry , vol.42 , pp. 3180-3188
    • Nield, J.1    Morris, E.P.2    Bibby, T.S.3    Barber, J.4
  • 51
    • 0035178383 scopus 로고    scopus 로고
    • Protein-protein interfaces: analysis of amino acid conservation in homodimers
    • Valdar W.S., and Thornton J.M. Protein-protein interfaces: analysis of amino acid conservation in homodimers. Proteins 42 (2001) 108-124
    • (2001) Proteins , vol.42 , pp. 108-124
    • Valdar, W.S.1    Thornton, J.M.2
  • 52
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: a plausible model
    • Monod J., Wyman J., and Changeux J.P. On the nature of allosteric transitions: a plausible model. J. Mol. Biol. 12 (1965) 88-118
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 53
    • 0032566696 scopus 로고    scopus 로고
    • Structural characterisation of apoflavodoxin shows that the location of the most stable nucleus differs among proteins with a flavodoxin-like topology
    • Steensma E., and van Mierlo C.P.M. Structural characterisation of apoflavodoxin shows that the location of the most stable nucleus differs among proteins with a flavodoxin-like topology. J. Mol. Biol. 282 (1998) 653-666
    • (1998) J. Mol. Biol. , vol.282 , pp. 653-666
    • Steensma, E.1    van Mierlo, C.P.M.2
  • 54
    • 0016840263 scopus 로고
    • Dimerization of Azotobacter vinelandii flavodoxin (azotoflavin)
    • Yoch D.C. Dimerization of Azotobacter vinelandii flavodoxin (azotoflavin). Arch. Biochem. Biophys. 170 (1975) 326-333
    • (1975) Arch. Biochem. Biophys. , vol.170 , pp. 326-333
    • Yoch, D.C.1
  • 56
    • 0031454750 scopus 로고    scopus 로고
    • A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution
    • Hoover D.M., and Ludwig M.L. A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution. Protein Sci. 6 (1997) 2525-2537
    • (1997) Protein Sci. , vol.6 , pp. 2525-2537
    • Hoover, D.M.1    Ludwig, M.L.2
  • 57
    • 0242592058 scopus 로고    scopus 로고
    • Can cofactor binding sites in proteins be flexible? Desulfovibrio desulfuricans flavodoxin binds FMN dimer
    • Muralidhara B.K., and Wittung-Stafshede P. Can cofactor binding sites in proteins be flexible? Desulfovibrio desulfuricans flavodoxin binds FMN dimer. Biochemistry 42 (2003) 13074-13080
    • (2003) Biochemistry , vol.42 , pp. 13074-13080
    • Muralidhara, B.K.1    Wittung-Stafshede, P.2
  • 58
    • 0026688841 scopus 로고
    • Crystal structure of oxidized flavodoxin from a red alga Chondrus crispus refined at 1.8 A resolution. Description of the flavin mononucleotide binding site
    • Fukuyama K., Matsubara H., and Rogers L.J. Crystal structure of oxidized flavodoxin from a red alga Chondrus crispus refined at 1.8 A resolution. Description of the flavin mononucleotide binding site. J. Mol. Biol. 225 (1992) 775-789
    • (1992) J. Mol. Biol. , vol.225 , pp. 775-789
    • Fukuyama, K.1    Matsubara, H.2    Rogers, L.J.3
  • 60
    • 0026513460 scopus 로고
    • Posttranslational modification of Klebsiella pneumoniae flavodoxin by covalent attachment of coenzyme A, shown by 31P NMR and electrospray mass spectrometry, prevents electron transfer from the nifJ protein to nitrogenase. A possible new regulatory mechanism for biological nitrogen fixation
    • Thorneley R.N., Abell C., Ashby G.A., Drummond M.H., Eady R.R., Huff S., Macdonald C.J., and Shneier A. Posttranslational modification of Klebsiella pneumoniae flavodoxin by covalent attachment of coenzyme A, shown by 31P NMR and electrospray mass spectrometry, prevents electron transfer from the nifJ protein to nitrogenase. A possible new regulatory mechanism for biological nitrogen fixation. Biochemistry 31 (1992) 1216-1224
    • (1992) Biochemistry , vol.31 , pp. 1216-1224
    • Thorneley, R.N.1    Abell, C.2    Ashby, G.A.3    Drummond, M.H.4    Eady, R.R.5    Huff, S.6    Macdonald, C.J.7    Shneier, A.8
  • 61
    • 0014027680 scopus 로고
    • Isolation and characteristics of flavodoxin from nitrogen-fixing Clostridium pasteurianum
    • Knight Jr. E., and Hardy R.W.F. Isolation and characteristics of flavodoxin from nitrogen-fixing Clostridium pasteurianum. J. Biol. Chem. 241 (1966) 2752-2756
    • (1966) J. Biol. Chem. , vol.241 , pp. 2752-2756
    • Knight Jr., E.1    Hardy, R.W.F.2
  • 62
    • 0014669476 scopus 로고
    • Purification and characterization of flavodoxin from Peptostreptococcus elsdenii
    • Mayhew S.G., and Massey V. Purification and characterization of flavodoxin from Peptostreptococcus elsdenii. J. Biol. Chem. 244 (1969) 794-803
    • (1969) J. Biol. Chem. , vol.244 , pp. 794-803
    • Mayhew, S.G.1    Massey, V.2
  • 63
    • 33748565349 scopus 로고    scopus 로고
    • Analytical ultracentrifugation for the study of protein association and assembly
    • Howlett G.J., Minton A.P., and Rivas G. Analytical ultracentrifugation for the study of protein association and assembly. Curr. Opin. Chem. Biol. 19 (2006) 430-436
    • (2006) Curr. Opin. Chem. Biol. , vol.19 , pp. 430-436
    • Howlett, G.J.1    Minton, A.P.2    Rivas, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.