메뉴 건너뛰기




Volumn 7, Issue 7, 2012, Pages

Cofactor binding protects flavodoxin against oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

4 CHLORO 7 NITROBENZOFURAZAN; APOFLAVODOXIN; CYSTEIC ACID; CYSTEINE; CYSTEINE 69; CYSTEINE SULFINIC ACID; DISULFIDE; DITHIOTHREITOL; FLAVODOXIN; HYDROGEN PEROXIDE; QUERCETIN; SULFENIC ACID DERIVATIVE; THIOL; UNCLASSIFIED DRUG;

EID: 84864066091     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0041363     Document Type: Article
Times cited : (10)

References (56)
  • 1
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • Ames BN, Shigenaga MK, Hagen TM, (1993) Oxidants, antioxidants, and the degenerative diseases of aging. Proc Natl Acad Sci U S A 90: 7915-7922.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 2
    • 0030952676 scopus 로고    scopus 로고
    • Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems
    • Chao CC, Ma YS, Stadtman ER, (1997) Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems. Proc Natl Acad Sci U S A 94: 2969-2974.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2969-2974
    • Chao, C.C.1    Ma, Y.S.2    Stadtman, E.R.3
  • 3
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman ER, Berlett BS, (1998) Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab Rev 30: 225-243.
    • (1998) Drug Metab Rev , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 5
    • 84863116671 scopus 로고    scopus 로고
    • Redox Sensing by Proteins: Oxidative Modifications on Cysteines and the Consequent Events
    • Wang Y, Yang J, Yi J, (2011) Redox Sensing by Proteins: Oxidative Modifications on Cysteines and the Consequent Events. Antioxidants & redox signaling 16: 649-657.
    • (2011) Antioxidants & Redox Signaling , vol.16 , pp. 649-657
    • Wang, Y.1    Yang, J.2    Yi, J.3
  • 6
    • 0026769401 scopus 로고
    • Reaction of Ozone with Glycophorin in Solution and in Lipid Vesicles
    • Banerjee SK, Mudd JB, (1992) Reaction of Ozone with Glycophorin in Solution and in Lipid Vesicles. Arch Biochem Biophys 295: 84-89.
    • (1992) Arch Biochem Biophys , vol.295 , pp. 84-89
    • Banerjee, S.K.1    Mudd, J.B.2
  • 8
    • 0035818520 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals
    • Moskovitz J, Bar-Noy S, Williams WM, Requena J, Berlett BS, et al. (2001) Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc Natl Acad Sci U S A 98: 12920-12925.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 12920-12925
    • Moskovitz, J.1    Bar-Noy, S.2    Williams, W.M.3    Requena, J.4    Berlett, B.S.5
  • 9
    • 47749151115 scopus 로고    scopus 로고
    • Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage
    • Cabreiro F, Picot CR, Perichon M, Castel J, Friguet B, et al. (2008) Overexpression of mitochondrial methionine sulfoxide reductase B2 protects leukemia cells from oxidative stress-induced cell death and protein damage. J Biol Chem 283: 16673-16681.
    • (2008) J Biol Chem , vol.283 , pp. 16673-16681
    • Cabreiro, F.1    Picot, C.R.2    Perichon, M.3    Castel, J.4    Friguet, B.5
  • 11
    • 78649847916 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A down-regulation in human breast cancer cells results in a more aggressive phenotype
    • De Luca A, Sanna F, Sallese M, Ruggiero C, Grossi M, et al. (2010) Methionine sulfoxide reductase A down-regulation in human breast cancer cells results in a more aggressive phenotype. Proc Natl Acad Sci U S A 107: 18628-18633.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 18628-18633
    • de Luca, A.1    Sanna, F.2    Sallese, M.3    Ruggiero, C.4    Grossi, M.5
  • 12
    • 78650078496 scopus 로고    scopus 로고
    • Quantitative reactivity profiling predicts functional cysteines in proteomes
    • Weerapana E, Wang C, Simon GM, Richter F, Khare S, et al. (2010) Quantitative reactivity profiling predicts functional cysteines in proteomes. Nature 468: 790-795.
    • (2010) Nature , vol.468 , pp. 790-795
    • Weerapana, E.1    Wang, C.2    Simon, G.M.3    Richter, F.4    Khare, S.5
  • 13
    • 0014590370 scopus 로고
    • Mechanism of peroxide-inactivation of the sulphydryl enzyme glyceraldehyde-3-phosphate dehydrogenase
    • Little C, O'Brien PJ, (1969) Mechanism of peroxide-inactivation of the sulphydryl enzyme glyceraldehyde-3-phosphate dehydrogenase. Eur J Biochem 10: 533-538.
    • (1969) Eur J Biochem , vol.10 , pp. 533-538
    • Little, C.1    O'Brien, P.J.2
  • 14
    • 0001637467 scopus 로고
    • Formation and reactions of sulfenic acids in proteins
    • Allison WS, (1976) Formation and reactions of sulfenic acids in proteins. Acc Chem Res 9: 293-299.
    • (1976) Acc Chem Res , vol.9 , pp. 293-299
    • Allison, W.S.1
  • 15
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • Claiborne A, Miller H, Parsonage D, Ross RP, (1993) Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation. Faseb J 7: 1483-1490.
    • (1993) Faseb J , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 16
    • 0033598677 scopus 로고    scopus 로고
    • Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation
    • Claiborne A, Yeh JI, Mallett TC, Luba J, Crane EJ 3rd, et al (1999) Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. Biochemistry 38: 15407-15416.
    • (1999) Biochemistry , vol.38 , pp. 15407-15416
    • Claiborne, A.1    Yeh, J.I.2    Mallett, T.C.3    Luba, J.4    Crane 3rd, E.J.5
  • 17
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • Saurin AT, Neubert H, Brennan JP, Eaton P, (2004) Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc Natl Acad Sci U S A 101: 17982-17987.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 17982-17987
    • Saurin, A.T.1    Neubert, H.2    Brennan, J.P.3    Eaton, P.4
  • 18
    • 79851510345 scopus 로고    scopus 로고
    • Chemical 'omics' approaches for understanding protein cysteine oxidation in biology
    • Leonard SE, Carroll KS, (2011) Chemical 'omics' approaches for understanding protein cysteine oxidation in biology. Curr Opin Chem Biol 15: 88-102.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 88-102
    • Leonard, S.E.1    Carroll, K.S.2
  • 19
    • 77955640917 scopus 로고    scopus 로고
    • Mapping protein cysteine sulfonic acid modifications with specific enrichment and mass spectrometry: an integrated approach to explore the cysteine oxidation
    • Chang YC, Huang CN, Lin CH, Chang HC, Wu CC, (2010) Mapping protein cysteine sulfonic acid modifications with specific enrichment and mass spectrometry: an integrated approach to explore the cysteine oxidation. Proteomics 10: 2961-2971.
    • (2010) Proteomics , vol.10 , pp. 2961-2971
    • Chang, Y.C.1    Huang, C.N.2    Lin, C.H.3    Chang, H.C.4    Wu, C.C.5
  • 21
    • 79953185783 scopus 로고    scopus 로고
    • Novel oxidative modifications in redox-active cysteine residues
    • Jeong J, Jung Y, Na S, Jeong J, Lee E, et al. (2011) Novel oxidative modifications in redox-active cysteine residues. Mol Cell Proteomics 10: M110.0005131-00051313.
    • (2011) Mol Cell Proteomics , vol.10
    • Jeong, J.1    Jung, Y.2    Na, S.3    Jeong, J.4    Lee, E.5
  • 22
    • 0023658381 scopus 로고
    • The elucidation of the microheterogeneity of highly purified p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by various biochemical techniques
    • Van Berkel WJ, Müller F, (1987) The elucidation of the microheterogeneity of highly purified p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens by various biochemical techniques. Eur J Biochem 167: 35-46.
    • (1987) Eur J Biochem , vol.167 , pp. 35-46
    • van Berkel, W.J.1    Müller, F.2
  • 23
    • 0036363570 scopus 로고    scopus 로고
    • Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins
    • Hamann M, Zhang T, Hendrich S, Thomas JA, (2002) Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins. Methods Enzymol 348: 146-156.
    • (2002) Methods Enzymol , vol.348 , pp. 146-156
    • Hamann, M.1    Zhang, T.2    Hendrich, S.3    Thomas, J.A.4
  • 24
    • 26944462004 scopus 로고    scopus 로고
    • Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis
    • Hochgrafe F, Mostertz J, Albrecht D, Hecker M, (2005) Fluorescence thiol modification assay: oxidatively modified proteins in Bacillus subtilis. Mol Microbiol 58: 409-425.
    • (2005) Mol Microbiol , vol.58 , pp. 409-425
    • Hochgrafe, F.1    Mostertz, J.2    Albrecht, D.3    Hecker, M.4
  • 25
    • 0025647850 scopus 로고
    • Engineering of microheterogeneity-resistant p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens
    • Eschrich K, van Berkel WJ, Westphal AH, de Kok A, Mattevi A, et al. (1990) Engineering of microheterogeneity-resistant p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. FEBS Lett 277: 197-199.
    • (1990) FEBS Lett , vol.277 , pp. 197-199
    • Eschrich, K.1    van Berkel, W.J.2    Westphal, A.H.3    de Kok, A.4    Mattevi, A.5
  • 26
    • 29144528214 scopus 로고    scopus 로고
    • Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences
    • Slavica A, Dib I, Nidetzky B, (2005) Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences. Appl Environ Microbiol 71: 8061-8068.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 8061-8068
    • Slavica, A.1    Dib, I.2    Nidetzky, B.3
  • 27
    • 0242668688 scopus 로고    scopus 로고
    • Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation
    • Woo HA, Chae HZ, Hwang SC, Yang KS, Kang SW, et al. (2003) Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation. Science 300: 653-656.
    • (2003) Science , vol.300 , pp. 653-656
    • Woo, H.A.1    Chae, H.Z.2    Hwang, S.C.3    Yang, K.S.4    Kang, S.W.5
  • 28
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu X, Kassim SY, Parks WC, Heinecke JW, (2001) Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J Biol Chem 276: 41279-41287.
    • (2001) J Biol Chem , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 29
    • 0014597950 scopus 로고
    • The electron transport system in nitrogen fixation by Azotobacter. I. Azotoflavin as an electron carrier
    • Benemann JR, Yoch DC, Valentine RC, Arnon DI, (1969) The electron transport system in nitrogen fixation by Azotobacter. I. Azotoflavin as an electron carrier. Proc Natl Acad Sci U S A 64: 1079-1086.
    • (1969) Proc Natl Acad Sci U S A , vol.64 , pp. 1079-1086
    • Benemann, J.R.1    Yoch, D.C.2    Valentine, R.C.3    Arnon, D.I.4
  • 30
    • 24344449928 scopus 로고    scopus 로고
    • A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: structural determinants of redox potential
    • Alagaratnam S, van Pouderoyen G, Pijning T, Dijkstra BW, Cavazzini D, et al. (2005) A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: structural determinants of redox potential. Protein Sci 14: 2284-2295.
    • (2005) Protein Sci , vol.14 , pp. 2284-2295
    • Alagaratnam, S.1    van Pouderoyen, G.2    Pijning, T.3    Dijkstra, B.W.4    Cavazzini, D.5
  • 31
    • 4043074820 scopus 로고    scopus 로고
    • Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin
    • Bollen YJ, Sanchéz IE, van Mierlo CP, (2004) Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin. Biochemistry 43: 10475-10489.
    • (2004) Biochemistry , vol.43 , pp. 10475-10489
    • Bollen, Y.J.1    Sanchéz, I.E.2    van Mierlo, C.P.3
  • 32
    • 17144415198 scopus 로고    scopus 로고
    • Protein topology affects the appearance of intermediates during the folding of proteins with a flavodoxin-like fold
    • Bollen YJ, van Mierlo CP, (2005) Protein topology affects the appearance of intermediates during the folding of proteins with a flavodoxin-like fold. Biophys Chem 114: 181-189.
    • (2005) Biophys Chem , vol.114 , pp. 181-189
    • Bollen, Y.J.1    van Mierlo, C.P.2
  • 33
    • 14844322304 scopus 로고    scopus 로고
    • Last in, first out: The role of cofactor binding in flavodoxin folding
    • Bollen YJ, Nabuurs SM, van Berkel WJ, van Mierlo CP, (2005) Last in, first out: The role of cofactor binding in flavodoxin folding. J Biol Chem 280: 7836-7844.
    • (2005) J Biol Chem , vol.280 , pp. 7836-7844
    • Bollen, Y.J.1    Nabuurs, S.M.2    van Berkel, W.J.3    van Mierlo, C.P.4
  • 34
    • 33645217096 scopus 로고    scopus 로고
    • The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates
    • Bollen YJ, Kamphuis MB, van Mierlo CP, (2006) The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates. Proc Natl Acad Sci U S A 103: 4095-4100.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4095-4100
    • Bollen, Y.J.1    Kamphuis, M.B.2    van Mierlo, C.P.3
  • 35
    • 58049200780 scopus 로고    scopus 로고
    • Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules
    • Nabuurs SM, Westphal AH, van Mierlo CP, (2008) Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules. J Am Chem Soc 130: 16914-16920.
    • (2008) J Am Chem Soc , vol.130 , pp. 16914-16920
    • Nabuurs, S.M.1    Westphal, A.H.2    van Mierlo, C.P.3
  • 36
    • 55549084888 scopus 로고    scopus 로고
    • Macromolecular crowding compacts unfolded apoflavodoxin and causes severe aggregation of the off-pathway intermediate during apoflavodoxin folding
    • Engel R, Westphal AH, Huberts DH, Nabuurs SM, Lindhoud S, et al. (2008) Macromolecular crowding compacts unfolded apoflavodoxin and causes severe aggregation of the off-pathway intermediate during apoflavodoxin folding. J Biol Chem 283: 27383-27394.
    • (2008) J Biol Chem , vol.283 , pp. 27383-27394
    • Engel, R.1    Westphal, A.H.2    Huberts, D.H.3    Nabuurs, S.M.4    Lindhoud, S.5
  • 37
    • 67749133718 scopus 로고    scopus 로고
    • Non-cooperative formation of the off-pathway molten globule during folding of the α-β parallel protein apoflavodoxin
    • Nabuurs SM, Westphal AH, van Mierlo CP, (2009) Non-cooperative formation of the off-pathway molten globule during folding of the α-β parallel protein apoflavodoxin. J Am Chem Soc 131: 2739-2746.
    • (2009) J Am Chem Soc , vol.131 , pp. 2739-2746
    • Nabuurs, S.M.1    Westphal, A.H.2    van Mierlo, C.P.3
  • 39
    • 0030167588 scopus 로고    scopus 로고
    • Possible role of a short extra loop of the long-chain flavodoxin from Azotobacter chroococcum in electron transfer to nitrogenase: complete 1H, 15N and 13C backbone assignments and secondary solution structure of the flavodoxin
    • Peelen S, Wijmenga S, Erbel PJ, Robson RL, Eady RR, et al. (1996) Possible role of a short extra loop of the long-chain flavodoxin from Azotobacter chroococcum in electron transfer to nitrogenase: complete 1H, 15N and 13C backbone assignments and secondary solution structure of the flavodoxin. J Biomol NMR 7: 315-330.
    • (1996) J Biomol NMR , vol.7 , pp. 315-330
    • Peelen, S.1    Wijmenga, S.2    Erbel, P.J.3    Robson, R.L.4    Eady, R.R.5
  • 40
    • 0016840263 scopus 로고
    • Dimerization of Azotobacter vinelandii flavodoxin (azotoflavin)
    • Yoch DC, (1975) Dimerization of Azotobacter vinelandii flavodoxin (azotoflavin). Arch Biochem Biophys 170: 326-333.
    • (1975) Arch Biochem Biophys , vol.170 , pp. 326-333
    • Yoch, D.C.1
  • 41
    • 0017382179 scopus 로고
    • Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii
    • Tanaka M, Haniu M, Yasunobu KT, Yoch DC, (1977) Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii. Biochemistry 16: 3525-3537.
    • (1977) Biochemistry , vol.16 , pp. 3525-3537
    • Tanaka, M.1    Haniu, M.2    Yasunobu, K.T.3    Yoch, D.C.4
  • 42
    • 0030060586 scopus 로고    scopus 로고
    • Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy
    • Steensma E, Heering HA, Hagen WR, Van Mierlo CP, (1996) Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy. Eur J Biochem 235: 167-172.
    • (1996) Eur J Biochem , vol.235 , pp. 167-172
    • Steensma, E.1    Heering, H.A.2    Hagen, W.R.3    van Mierlo, C.P.4
  • 44
    • 0032566696 scopus 로고    scopus 로고
    • Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology
    • Steensma E, van Mierlo CP, (1998) Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology. J Mol Biol 282: 653-666.
    • (1998) J Mol Biol , vol.282 , pp. 653-666
    • Steensma, E.1    van Mierlo, C.P.2
  • 45
    • 66649083142 scopus 로고    scopus 로고
    • Galactonolactone dehydrogenase requires a redox-sensitive thiol for optimal production of vitamin C
    • Leferink NG, van Duijn E, Barendregt A, Heck AJ, van Berkel WJ, (2009) Galactonolactone dehydrogenase requires a redox-sensitive thiol for optimal production of vitamin C. Plant Physiol 150: 596-605.
    • (2009) Plant Physiol , vol.150 , pp. 596-605
    • Leferink, N.G.1    van Duijn, E.2    Barendregt, A.3    Heck, A.J.4    van Berkel, W.J.5
  • 46
    • 0036371370 scopus 로고    scopus 로고
    • Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase
    • Poole LB, Ellis HR, (2002) Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase. Methods Enzymol 348: 122-136.
    • (2002) Methods Enzymol , vol.348 , pp. 122-136
    • Poole, L.B.1    Ellis, H.R.2
  • 47
    • 0030778083 scopus 로고    scopus 로고
    • Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase
    • Ellis HR, Poole LB, (1997) Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase. Biochemistry 36: 15013-15018.
    • (1997) Biochemistry , vol.36 , pp. 15013-15018
    • Ellis, H.R.1    Poole, L.B.2
  • 48
    • 56149087277 scopus 로고    scopus 로고
    • Native mass spectrometry: a bridge between interactomics and structural biology
    • Heck AJR, (2008) Native mass spectrometry: a bridge between interactomics and structural biology. Nat Methods 5: 927-933.
    • (2008) Nat Methods , vol.5 , pp. 927-933
    • Heck, A.J.R.1
  • 49
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation
    • Denu JM, Tanner KG, (1998) Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. Biochemistry 37: 5633-5642.
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 50
    • 0242267926 scopus 로고    scopus 로고
    • Deflavination and reconstitution of flavoproteins
    • Hefti MH, Vervoort J, van Berkel WJ, (2003) Deflavination and reconstitution of flavoproteins. Eur J Biochem 270: 4227-4242.
    • (2003) Eur J Biochem , vol.270 , pp. 4227-4242
    • Hefti, M.H.1    Vervoort, J.2    van Berkel, W.J.3
  • 52
    • 0031952923 scopus 로고    scopus 로고
    • Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding
    • Steensma E, Nijman MJ, Bollen YJ, de Jager PA, van den Berg WA, et al. (1998) Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding. Protein Sci 7: 306-317.
    • (1998) Protein Sci , vol.7 , pp. 306-317
    • Steensma, E.1    Nijman, M.J.2    Bollen, Y.J.3    de Jager, P.A.4    van den Berg, W.A.5
  • 53
    • 0034717064 scopus 로고    scopus 로고
    • Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story
    • van Mierlo CP, Steensma E, (2000) Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story. J Biotechnol 79: 281-298.
    • (2000) J Biotechnol , vol.79 , pp. 281-298
    • van Mierlo, C.P.1    Steensma, E.2
  • 54
    • 0031792027 scopus 로고    scopus 로고
    • The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate
    • van Mierlo CP, van Dongen WM, Vergeldt F, van Berkel WJ, Steensma E, (1998) The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate. Protein Sci 7: 2331-2344.
    • (1998) Protein Sci , vol.7 , pp. 2331-2344
    • van Mierlo, C.P.1    van Dongen, W.M.2    Vergeldt, F.3    van Berkel, W.J.4    Steensma, E.5
  • 55
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman GL, (1959) Tissue sulfhydryl groups. Arch Biochem Biophys 82: 70-77.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 56
    • 77957001732 scopus 로고
    • Reaction of protein sulfhydryl groups with Ellman's reagent
    • Habeeb AFSA, (1972) Reaction of protein sulfhydryl groups with Ellman's reagent. Methods Enzymol 25: 457-464.
    • (1972) Methods Enzymol , vol.25 , pp. 457-464
    • Habeeb, A.F.S.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.