메뉴 건너뛰기




Volumn 392, Issue 2, 2009, Pages 436-451

Specific Interactions between the Ferredoxin and Terminal Oxygenase Components of a Class IIB Rieske Nonheme Iron Oxygenase, Carbazole 1,9a-Dioxygenase

Author keywords

carbazole; electron transfer; protein protein interaction; Rieske nonheme iron oxygenase; 2Fe 2S cluster

Indexed keywords

CARBAZOLE 1,9A DIOXYGENASE; FERREDOXIN; FLAVINE ADENINE NUCLEOTIDE; GLUTAMIC ACID; HISTIDINE; IRON SULFUR PROTEIN; LEUCINE; LYSINE; NONHEME IRON PROTEIN; OXYGENASE; PHENYLALANINE; PROLINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; TRYPTOPHAN; UNCLASSIFIED DRUG; VALINE;

EID: 68949212842     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.07.029     Document Type: Article
Times cited : (27)

References (52)
  • 1
    • 0026743341 scopus 로고
    • The electron-transport proteins of hydroxylating bacterial dioxygenases
    • Mason J.R., and Cammack R. The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu. Rev. Microbiol. 46 (1992) 277-305
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 277-305
    • Mason, J.R.1    Cammack, R.2
  • 2
    • 0000843661 scopus 로고    scopus 로고
    • Molecular bases of aerobic bacterial degradation of dioxins: involvement of angular dioxygenation
    • Nojiri H., and Omori T. Molecular bases of aerobic bacterial degradation of dioxins: involvement of angular dioxygenation. Biosci. Biotechnol. Biochem. 66 (2002) 2001-2016
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2001-2016
    • Nojiri, H.1    Omori, T.2
  • 3
    • 0002557598 scopus 로고
    • Phthalate dioxygenase reductase and related flavin-iron-sulfur containing electron transferases
    • Muller F. (Ed), CRC Press, Boca Raton, FL
    • Batie C.J., Ballou D.P., and Correll C.C. Phthalate dioxygenase reductase and related flavin-iron-sulfur containing electron transferases. In: Muller F. (Ed). Chemistry and Biochemistry of Flavoenzymes vol. 3 (1991), CRC Press, Boca Raton, FL 543-556
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 543-556
    • Batie, C.J.1    Ballou, D.P.2    Correll, C.C.3
  • 4
    • 27544477399 scopus 로고    scopus 로고
    • Rieske business: structure-function of Rieske non-heme oxygenases
    • Ferraro D.J., Gakhar L., and Ramaswamy S. Rieske business: structure-function of Rieske non-heme oxygenases. Biochem. Biophys. Res. Commun. 338 (2005) 175-190
    • (2005) Biochem. Biophys. Res. Commun. , vol.338 , pp. 175-190
    • Ferraro, D.J.1    Gakhar, L.2    Ramaswamy, S.3
  • 5
    • 58149094956 scopus 로고    scopus 로고
    • Carbazole metabolism by pseudomonads
    • Ramos J.-L., and Filloux A. (Eds), Springer, New York, NY
    • Nojiri H., and Omori T. Carbazole metabolism by pseudomonads. In: Ramos J.-L., and Filloux A. (Eds). Pseudomonas vol. 5 (2007), Springer, New York, NY 107-145
    • (2007) Pseudomonas , vol.5 , pp. 107-145
    • Nojiri, H.1    Omori, T.2
  • 6
    • 19944426997 scopus 로고    scopus 로고
    • Divergent structures of carbazole degradative car operons isolated from gram-negative bacteria
    • Inoue K., Widada J., Nakai S., Endoh T., Urata M., Ashikawa Y., et al. Divergent structures of carbazole degradative car operons isolated from gram-negative bacteria. Biosci. Biotechnol. Biochem. 68 (2004) 1467-1480
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 1467-1480
    • Inoue, K.1    Widada, J.2    Nakai, S.3    Endoh, T.4    Urata, M.5    Ashikawa, Y.6
  • 7
    • 15744395874 scopus 로고    scopus 로고
    • Diversity of carbazole-degrading bacteria having the car gene cluster: isolation of a novel gram-positive carbazole-degrading bacterium
    • Inoue K., Habe H., Yamane H., Omori T., and Nojiri H. Diversity of carbazole-degrading bacteria having the car gene cluster: isolation of a novel gram-positive carbazole-degrading bacterium. FEMS Microbiol. Lett. 245 (2005) 145-153
    • (2005) FEMS Microbiol. Lett. , vol.245 , pp. 145-153
    • Inoue, K.1    Habe, H.2    Yamane, H.3    Omori, T.4    Nojiri, H.5
  • 8
    • 0030744612 scopus 로고    scopus 로고
    • Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10
    • Sato S., Nam J.-W., Kasuga K., Nojiri H., Yamane H., and Omori T. Identification and characterization of genes encoding carbazole 1,9a-dioxygenase in Pseudomonas sp. strain CA10. J. Bacteriol. 179 (1997) 4850-4858
    • (1997) J. Bacteriol. , vol.179 , pp. 4850-4858
    • Sato, S.1    Nam, J.-W.2    Kasuga, K.3    Nojiri, H.4    Yamane, H.5    Omori, T.6
  • 9
    • 33646561203 scopus 로고    scopus 로고
    • Characterization of novel carbazole catabolism genes from gram-positive carbazole degrader Nocardioides aromaticivorans IC177
    • Inoue K., Habe H., Yamane H., and Nojiri H. Characterization of novel carbazole catabolism genes from gram-positive carbazole degrader Nocardioides aromaticivorans IC177. Appl. Environ. Microbiol. 72 (2006) 3321-3329
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3321-3329
    • Inoue, K.1    Habe, H.2    Yamane, H.3    Nojiri, H.4
  • 10
    • 33646562479 scopus 로고    scopus 로고
    • Plasmid pCAR3 contains multiple gene sets involved in the conversion of carbazole to anthranilate
    • Urata M., Uchimura H., Noguchi H., Sakaguchi T., Takemura T., Eto K., et al. Plasmid pCAR3 contains multiple gene sets involved in the conversion of carbazole to anthranilate. Appl. Environ. Microbiol. 72 (2006) 3198-3205
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 3198-3205
    • Urata, M.1    Uchimura, H.2    Noguchi, H.3    Sakaguchi, T.4    Takemura, T.5    Eto, K.6
  • 11
    • 22444433648 scopus 로고    scopus 로고
    • Structure of the terminal oxygenase component of angular dioxygenase, carbazole 1,9a-dioxygenase
    • Nojiri H., Ashikawa Y., Noguchi H., Nam J.-W., Urata M., Fujimoto Z., et al. Structure of the terminal oxygenase component of angular dioxygenase, carbazole 1,9a-dioxygenase. J. Mol. Biol. 351 (2005) 355-370
    • (2005) J. Mol. Biol. , vol.351 , pp. 355-370
    • Nojiri, H.1    Ashikawa, Y.2    Noguchi, H.3    Nam, J.-W.4    Urata, M.5    Fujimoto, Z.6
  • 12
    • 13944256249 scopus 로고    scopus 로고
    • Crystal structure of the ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-heme iron oxygenase system
    • Nam J.-W., Noguchi H., Fujimoto Z., Mizuno H., Ashikawa Y., Abo M., et al. Crystal structure of the ferredoxin component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10, a novel Rieske non-heme iron oxygenase system. Proteins 58 (2005) 779-789
    • (2005) Proteins , vol.58 , pp. 779-789
    • Nam, J.-W.1    Noguchi, H.2    Fujimoto, Z.3    Mizuno, H.4    Ashikawa, Y.5    Abo, M.6
  • 13
    • 33845229149 scopus 로고    scopus 로고
    • Electron transfer complex formation between oxygenase and ferredoxin components in Rieske nonheme iron oxygenase system
    • Ashikawa Y., Fujimoto Z., Noguchi H., Habe H., Omori T., Yamane H., and Nojiri H. Electron transfer complex formation between oxygenase and ferredoxin components in Rieske nonheme iron oxygenase system. Structure 14 (2006) 1779-1789
    • (2006) Structure , vol.14 , pp. 1779-1789
    • Ashikawa, Y.1    Fujimoto, Z.2    Noguchi, H.3    Habe, H.4    Omori, T.5    Yamane, H.6    Nojiri, H.7
  • 14
    • 0036947146 scopus 로고    scopus 로고
    • Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10
    • Nam J.-W., Nojiri H., Noguchi H., Uchimura H., Yoshida T., Habe H., et al. Purification and characterization of carbazole 1,9a-dioxygenase, a three-component dioxygenase system of Pseudomonas resinovorans strain CA10. Appl. Environ. Microbiol. 68 (2002) 5882-5890
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5882-5890
    • Nam, J.-W.1    Nojiri, H.2    Noguchi, H.3    Uchimura, H.4    Yoshida, T.5    Habe, H.6
  • 15
    • 0021895134 scopus 로고
    • Purification and properties of ferredoxinTOL. A component of toluene dioxygenase from Pseudomonas putida F1
    • Subramanian V., Liu T.-N., Yeh W.-K., Serdar C.M., Wrackett L.P., and Gibson D.T. Purification and properties of ferredoxinTOL. A component of toluene dioxygenase from Pseudomonas putida F1. J. Biol. Chem. 260 (1985) 2355-2363
    • (1985) J. Biol. Chem. , vol.260 , pp. 2355-2363
    • Subramanian, V.1    Liu, T.-N.2    Yeh, W.-K.3    Serdar, C.M.4    Wrackett, L.P.5    Gibson, D.T.6
  • 16
    • 0028865344 scopus 로고
    • Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components
    • Hurtubise Y., Barriault D., Powlowski J., and Sylvestre M. Purification and characterization of the Comamonas testosteroni B-356 biphenyl dioxygenase components. J. Bacteriol. 177 (1995) 6610-6618
    • (1995) J. Bacteriol. , vol.177 , pp. 6610-6618
    • Hurtubise, Y.1    Barriault, D.2    Powlowski, J.3    Sylvestre, M.4
  • 17
    • 0033024795 scopus 로고    scopus 로고
    • Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase
    • Barriault D., and Sylvestre M. Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase. Appl. Microbiol. Biotechnol. 51 (1999) 592-597
    • (1999) Appl. Microbiol. Biotechnol. , vol.51 , pp. 592-597
    • Barriault, D.1    Sylvestre, M.2
  • 18
    • 0021378817 scopus 로고
    • An investigation of the iron-sulphur proteins of benzene dioxygenase from Pseudomonas putida by electron-spin-resonance spectroscopy
    • Geary P.J., Saboowalla F., Patil D., and Cammack R. An investigation of the iron-sulphur proteins of benzene dioxygenase from Pseudomonas putida by electron-spin-resonance spectroscopy. Biochem. J. 217 (1984) 667-673
    • (1984) Biochem. J. , vol.217 , pp. 667-673
    • Geary, P.J.1    Saboowalla, F.2    Patil, D.3    Cammack, R.4
  • 20
    • 33846687102 scopus 로고    scopus 로고
    • Redox and functional analysis of the Rieske ferredoxin component of the toluene 4-monooxygenase
    • Elsen N.L., Moe L.A., McMartin L.A., and Fox B.G. Redox and functional analysis of the Rieske ferredoxin component of the toluene 4-monooxygenase. Biochemistry 46 (2007) 976-986
    • (2007) Biochemistry , vol.46 , pp. 976-986
    • Elsen, N.L.1    Moe, L.A.2    McMartin, L.A.3    Fox, B.G.4
  • 22
    • 0031574021 scopus 로고    scopus 로고
    • Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein
    • Carrell C.J., Zhang H., Cramer W.A., and Smith J.L. Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein. Structure 5 (1997) 1613-1625
    • (1997) Structure , vol.5 , pp. 1613-1625
    • Carrell, C.J.1    Zhang, H.2    Cramer, W.A.3    Smith, J.L.4
  • 23
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • Colbert C.L., Couture M.M.J., Eltis L.D., and Bolin J.T. A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure 8 (2000) 1267-1278
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.L.1    Couture, M.M.J.2    Eltis, L.D.3    Bolin, J.T.4
  • 24
    • 34047222146 scopus 로고    scopus 로고
    • Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1
    • Ferraro D.J., Brown E.N., Yu C.-L., Parales R.E., Gibson D.T., and Ramaswamy S. Structural investigations of the ferredoxin and terminal oxygenase components of the biphenyl 2,3-dioxygenase from Sphingobium yanoikuyae B1. BMC Struct. Biol. 7 (2007) 10
    • (2007) BMC Struct. Biol. , vol.7 , pp. 10
    • Ferraro, D.J.1    Brown, E.N.2    Yu, C.-L.3    Parales, R.E.4    Gibson, D.T.5    Ramaswamy, S.6
  • 25
    • 34548836830 scopus 로고    scopus 로고
    • Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S] ferredoxin
    • Senda M., Kishigami S., Kimura S., Fukuda M., Ishida T., and Senda T. Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S] ferredoxin. J. Mol. Biol. 373 (2007) 382-400
    • (2007) J. Mol. Biol. , vol.373 , pp. 382-400
    • Senda, M.1    Kishigami, S.2    Kimura, S.3    Fukuda, M.4    Ishida, T.5    Senda, T.6
  • 26
    • 0029055861 scopus 로고
    • Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 Å resolution: structural comparisons of plant-type ferredoxins and an electrostatic potential analysis
    • Fukuyama K., Ueki N., Nakamura H., Tsukihara T., and Matsubara H. Tertiary structure of [2Fe-2S] ferredoxin from Spirulina platensis refined at 2.5 Å resolution: structural comparisons of plant-type ferredoxins and an electrostatic potential analysis. J. Biochem. 117 (1995) 1017-1023
    • (1995) J. Biochem. , vol.117 , pp. 1017-1023
    • Fukuyama, K.1    Ueki, N.2    Nakamura, H.3    Tsukihara, T.4    Matsubara, H.5
  • 27
    • 0038746890 scopus 로고    scopus 로고
    • High-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparison
    • Hunsicker-Wang L.M., Heine A., Chen Y., Luna E.P., Todaro T., Zhang Y.M., et al. High-resolution structure of the soluble, respiratory-type Rieske protein from Thermus thermophilus: analysis and comparison. Biochemistry 42 (2003) 7303-7317
    • (2003) Biochemistry , vol.42 , pp. 7303-7317
    • Hunsicker-Wang, L.M.1    Heine, A.2    Chen, Y.3    Luna, E.P.4    Todaro, T.5    Zhang, Y.M.6
  • 28
    • 33846263979 scopus 로고    scopus 로고
    • Atomic resolution structures of Rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters
    • Kolling D.J., Brunzelle J.S., Lhee S., Crofts A.R., and Nair S.K. Atomic resolution structures of Rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters. Structure 15 (2007) 29-38
    • (2007) Structure , vol.15 , pp. 29-38
    • Kolling, D.J.1    Brunzelle, J.S.2    Lhee, S.3    Crofts, A.R.4    Nair, S.K.5
  • 31
    • 33845499915 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the terminal oxygenase component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177
    • Inoue K., Ashikawa Y., Usami Y., Noguchi H., Fujimoto Z., Yamane H., and Nojiri H. Crystallization and preliminary X-ray diffraction studies of the terminal oxygenase component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 62 (2006) 1212-1214
    • (2006) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.62 , pp. 1212-1214
    • Inoue, K.1    Ashikawa, Y.2    Usami, Y.3    Noguchi, H.4    Fujimoto, Z.5    Yamane, H.6    Nojiri, H.7
  • 32
    • 4444337310 scopus 로고    scopus 로고
    • Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1
    • Furusawa Y., Nagarajan V., Tanokura M., Masai E., Fukuda M., and Senda T. Crystal structure of the terminal oxygenase component of biphenyl dioxygenase derived from Rhodococcus sp. strain RHA1. J. Mol. Biol. 342 (2004) 1041-1052
    • (2004) J. Mol. Biol. , vol.342 , pp. 1041-1052
    • Furusawa, Y.1    Nagarajan, V.2    Tanokura, M.3    Masai, E.4    Fukuda, M.5    Senda, T.6
  • 34
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page C.C., Moser C.C., Chen X., and Dutton P.L. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402 (1999) 47-52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 35
    • 34848903250 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of the ferredoxin component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177
    • Inoue K., Ashikawa Y., Usami Y., Noguchi H., Fujimoto Z., Yamane H., and Nojiri H. Crystallization and preliminary crystallographic analysis of the ferredoxin component of carbazole 1,9a-dioxygenase from Nocardioides aromaticivorans IC177. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 63 (2007) 855-857
    • (2007) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.63 , pp. 855-857
    • Inoue, K.1    Ashikawa, Y.2    Usami, Y.3    Noguchi, H.4    Fujimoto, Z.5    Yamane, H.6    Nojiri, H.7
  • 36
    • 34249951772 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the ferredoxin reductase component in the Rieske nonhaem iron oxygenase system carbazole 1,9a-dioxygenase
    • Ashikawa Y., Uchimura H., Fujimoto Z., Inoue K., Noguchi H., Yamane H., and Nojiri H. Crystallization and preliminary X-ray diffraction studies of the ferredoxin reductase component in the Rieske nonhaem iron oxygenase system carbazole 1,9a-dioxygenase. Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. 63 (2007) 499-502
    • (2007) Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun. , vol.63 , pp. 499-502
    • Ashikawa, Y.1    Uchimura, H.2    Fujimoto, Z.3    Inoue, K.4    Noguchi, H.5    Yamane, H.6    Nojiri, H.7
  • 37
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 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
  • 41
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 47
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L., and Park J. DaliLite workbench for protein structure comparison. Bioinformatics 16 (2000) 566-567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 48
    • 0031715982 scopus 로고    scopus 로고
    • Protein structure alignment by incremental combinatorial extension (CE) of the optimal path
    • Shindyalov I.N., and Bourne P.E. Protein structure alignment by incremental combinatorial extension (CE) of the optimal path. Protein Eng. 11 (1998) 739-747
    • (1998) Protein Eng. , vol.11 , pp. 739-747
    • Shindyalov, I.N.1    Bourne, P.E.2
  • 49
  • 50
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: an automated docking and discrimination method for the prediction of protein complexes
    • Comeau S.R., Gatchell D.W., Vajda S., and Camacho C.J. ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20 (2004) 45-50
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 51
    • 0037080244 scopus 로고    scopus 로고
    • Rapid grid-based construction of the molecular surface and the use of induced surface charge to calculate reaction field energies: applications to the molecular systems and geometric objects
    • Rocchia W., Sricharan S., Nicholls A., Alexov E., Chabrera A., and Honig B. Rapid grid-based construction of the molecular surface and the use of induced surface charge to calculate reaction field energies: applications to the molecular systems and geometric objects. J. Comp. Chem. 23 (2002) 128-137
    • (2002) J. Comp. Chem. , vol.23 , pp. 128-137
    • Rocchia, W.1    Sricharan, S.2    Nicholls, A.3    Alexov, E.4    Chabrera, A.5    Honig, B.6
  • 52
    • 0026434593 scopus 로고
    • Protein electron transfer rates set by the bridging secondary and tertiary structure
    • Bertan D.N., Betts J.N., and Onuchic J.N. Protein electron transfer rates set by the bridging secondary and tertiary structure. Science 252 (1991) 1285-1288
    • (1991) Science , vol.252 , pp. 1285-1288
    • Bertan, D.N.1    Betts, J.N.2    Onuchic, J.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.