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Volumn 263, Issue 1, 1996, Pages 53-69

Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution

Author keywords

Crystal structure; Dimethyl sulfoxide reductase; Molecular replacement; Molybdopterin cofactor; Multiple isomorphous replacement

Indexed keywords

CYTOCHROME C; DIMETHYL SULFIDE; DIMETHYL SULFOXIDE; MOLYBDENUM; OXIDOREDUCTASE;

EID: 0030592449     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0555     Document Type: Article
Times cited : (259)

References (74)
  • 2
    • 84986786375 scopus 로고
    • Dimethylsulfoxide in marine and freshwaters
    • Andreae, M. O. (1980). Dimethylsulfoxide in marine and freshwaters. Limnol. Oceangr. 25, 1054-1063.
    • (1980) Limnol. Oceangr. , vol.25 , pp. 1054-1063
    • Andreae, M.O.1
  • 3
    • 0027412196 scopus 로고
    • ALSCRIPT: A tool to format multiple sequence alignments
    • Barton, G. J. (1993). ALSCRIPT: a tool to format multiple sequence alignments. Protein Eng. 6, 37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 4
    • 0027454258 scopus 로고
    • Aldehyde oxidoreductase activity in Desulfovibrio gigas: In vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen
    • Barata, B. A. S., LeGall, J. & Moura, J. J. G. (1993). Aldehyde oxidoreductase activity in Desulfovibrio gigas: in vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen. Biochemistry, 32, 11559-11568.
    • (1993) Biochemistry , vol.32 , pp. 11559-11568
    • Barata, B.A.S.1    LeGall, J.2    Moura, J.J.G.3
  • 5
    • 4244114939 scopus 로고
    • Characterization of the molybdopterin cofactor of DMSO/ TMAO reductase from rhodobacter shaeroides f. sp. denitrificans
    • Bastian, N. R. & Rajagopalan, K. V. (1988). Characterization of the molybdopterin cofactor of DMSO/ TMAO reductase from Rhodobacter shaeroides f. sp. denitrificans. J. Cell Biol. 107, 845a.
    • (1988) J. Cell Biol. , vol.107
    • Bastian, N.R.1    Rajagopalan, K.V.2
  • 6
    • 0026086008 scopus 로고
    • Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans
    • Bastian, N. R., Kay, C. J., Barber, M. J. & Rajagopalan, K. V. (1991). Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans. J. Biol. Chem. 266, 45-51.
    • (1991) J. Biol. Chem. , vol.266 , pp. 45-51
    • Bastian, N.R.1    Kay, C.J.2    Barber, M.J.3    Rajagopalan, K.V.4
  • 8
    • 0029064901 scopus 로고
    • Nitric oxide stabilizes the Mo(V) oxidation state of dimethyl sulfoxide reductase from Rhodobacter sphaeroides without inhibiting enzyme activity
    • Bastian, N. R., Foster, M. J. P. & Pope J. C. (1995). Nitric oxide stabilizes the Mo(V) oxidation state of dimethyl sulfoxide reductase from Rhodobacter sphaeroides without inhibiting enzyme activity. BioFactors, 5, 5-10.
    • (1995) BioFactors , vol.5 , pp. 5-10
    • Bastian, N.R.1    Foster, M.J.P.2    Pope, J.C.3
  • 9
    • 0028023353 scopus 로고
    • Multiple states of the molybdenum centre of dimethylsulfoxide reductase from Rhodobacter capsulatus revealed by EPR spectroscopy
    • Bennet, B., Benson, N., McEwan, A. G. & Bray, R. C. (1994). Multiple states of the molybdenum centre of dimethylsulfoxide reductase from Rhodobacter capsulatus revealed by EPR spectroscopy. Eur. J. Biochem. 225, 321-331.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 321-331
    • Bennet, B.1    Benson, N.2    McEwan, A.G.3    Bray, R.C.4
  • 10
    • 0026719264 scopus 로고
    • Detection of the optical bands of molybdenum(V) in DMSO reductase (Rhodobacter capsulatus) by low-temperature MCD spectroscopy
    • Benson, N., Farrar, J. A., McEwan, A. G. & Thomson, A. J. (1992). Detection of the optical bands of molybdenum(V) in DMSO reductase (Rhodobacter capsulatus) by low-temperature MCD spectroscopy. FEBS Letters, 307, 169-172.
    • (1992) FEBS Letters , vol.307 , pp. 169-172
    • Benson, N.1    Farrar, J.A.2    McEwan, A.G.3    Thomson, A.J.4
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 0024066828 scopus 로고
    • The inorganic biochemistry of molybdoenzymes
    • Bray, R. C. (1988). The inorganic biochemistry of molybdoenzymes. Quart. Rev. Biophys. 21, 299-329.
    • (1988) Quart. Rev. Biophys. , vol.21 , pp. 299-329
    • Bray, R.C.1
  • 14
    • 0024279342 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to a 2.8 Å resolution structure of aspartate aminotransferase
    • Brünger, A. T. (1988). Crystallographic refinement by simulated annealing: application to a 2.8 Å resolution structure of aspartate aminotransferase. J. Mol. Biol. 203, 803-816.
    • (1988) J. Mol. Biol. , vol.203 , pp. 803-816
    • Brünger, A.T.1
  • 15
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 16
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A. T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science, 35, 458-460.
    • (1987) Science , vol.35 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 17
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D, 50, 760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 18
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan, M. K., Swarnalatha, M., Kletzin, A., Adams, M. W. W. & Rees, D. C. (1995). Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science, 267, 1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Swarnalatha, M.2    Kletzin, A.3    Adams, M.W.W.4    Rees, D.C.5
  • 19
    • 0001736762 scopus 로고
    • Arsenite-inhibited xanthine oxidase - Determination of the Mo-S-As geometry by EXAFS
    • Cramer, S. P. & Hille, R. (1985). Arsenite-inhibited xanthine oxidase - determination of the Mo-S-As geometry by EXAFS. J. Am. Chem. Soc. 107, 8164-8169.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 8164-8169
    • Cramer, S.P.1    Hille, R.2
  • 20
    • 33845558282 scopus 로고
    • Molybdenum sites of sulfite oxidase and xanthine dehydrogenase: A comparison by EXAFS
    • Cramer, S. P., Wahl, R. & Rajagopalan, K. V. (1981). Molybdenum sites of sulfite oxidase and xanthine dehydrogenase: a comparison by EXAFS. J. Am. Chem. Soc. 103, 7721-7727.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7721-7727
    • Cramer, S.P.1    Wahl, R.2    Rajagopalan, K.V.3
  • 21
    • 0001380448 scopus 로고
    • Molybdenum sites of Escherichia coli and Chlorella vulgaris nitrate reductase: A comparison by EXAFS
    • Cramer, S. P., Solomonson, L. P., Adams, M. W. W. & Mortenson, L. E. (1984). Molybdenum sites of Escherichia coli and Chlorella vulgaris nitrate reductase: a comparison by EXAFS. J. Am. Chem. Soc. 106, 1467-1471.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 1467-1471
    • Cramer, S.P.1    Solomonson, L.P.2    Adams, M.W.W.3    Mortenson, L.E.4
  • 22
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A, 47, 392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 23
    • 0025200341 scopus 로고
    • The interaction of bisulphite with milk xanthine oxidase
    • Fish, K. M., Massey, V., Sands, R. H. & Dunham, W. R. (1990). The interaction of bisulphite with milk xanthine oxidase. J. Biol. Chem. 265, 19665-19671.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19665-19671
    • Fish, K.M.1    Massey, V.2    Sands, R.H.3    Dunham, W.R.4
  • 26
    • 0027489119 scopus 로고
    • Molybdopterin guanine dinucleotide is the organic moiety of the molybdenum cofactor in respiratory nitrate reductase from Pseudomonas stutzeri
    • Frunzke, K., Heiss, B., Meyer, O. & Zumft, W. G. (1993). Molybdopterin guanine dinucleotide is the organic moiety of the molybdenum cofactor in respiratory nitrate reductase from Pseudomonas stutzeri. FEMS Microbiol. Letters, 113, 241-246.
    • (1993) FEMS Microbiol. Letters , vol.113 , pp. 241-246
    • Frunzke, K.1    Heiss, B.2    Meyer, O.3    Zumft, W.G.4
  • 29
    • 0029926237 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy of dimethyl sulfoxide reductase from Rhodobacter sphaeroides
    • George, G. N., Hilton, J. & Rajagopalan, K. V. (1996). X-ray absorption spectroscopy of dimethyl sulfoxide reductase from Rhodobacter sphaeroides. J. Am. Chem. Soc. 118, 1113-1117.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1113-1117
    • George, G.N.1    Hilton, J.2    Rajagopalan, K.V.3
  • 30
    • 0002493329 scopus 로고
    • The occurrence and significans of trimethyl amine oxide in marine animals
    • Groninger, H. S. (1959). The occurrence and significans of trimethyl amine oxide in marine animals. US Fish. Wildl. Serv. Sci. Rep. Fish. 333, 1-22.
    • (1959) US Fish. Wildl. Serv. Sci. Rep. Fish. , vol.333 , pp. 1-22
    • Groninger, H.S.1
  • 31
    • 0018109126 scopus 로고
    • Comparison of the molybdenum centres of nativ and desulpho xanthine oxidase: The nature of the cyanide-labile sulphur atom and the nature of the proton-accepting group
    • Gutteridge, S., Tanner, S. J., & Bray, R. C. (1978). Comparison of the molybdenum centres of nativ and desulpho xanthine oxidase: the nature of the cyanide-labile sulphur atom and the nature of the proton-accepting group. Biochem. J. 175, 887-897.
    • (1978) Biochem. J. , vol.175 , pp. 887-897
    • Gutteridge, S.1    Tanner, S.J.2    Bray, R.C.3
  • 32
    • 0028202893 scopus 로고
    • The reaction mechanism of oxomolybdenum enzymes
    • Hille R. (1994). The reaction mechanism of oxomolybdenum enzymes. Biochim. Biophys. Acta, 1184, 143-169.
    • (1994) Biochim. Biophys. Acta , vol.1184 , pp. 143-169
    • Hille, R.1
  • 33
    • 0030012488 scopus 로고    scopus 로고
    • Molecular cloning of dimethyl sulfoxide reductase from Rhodobacter capsulatus
    • Hilton, J. & Rajagopalan, K. V. (1996). Molecular cloning of dimethyl sulfoxide reductase from Rhodobacter capsulatus. Biochim. Biophys. Acta, 1294, 111-114.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 111-114
    • Hilton, J.1    Rajagopalan, K.V.2
  • 35
    • 0017359130 scopus 로고
    • Tryptic cleavage of rat liver sulfite oxidase: Isolation and characterization of molybdenum and heme domains
    • Johnson, J. L. & Rajagopalan, K. V. (1977). Tryptic cleavage of rat liver sulfite oxidase: isolation and characterization of molybdenum and heme domains. J. Biol. Chem. 252, 2017-2025.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2017-2025
    • Johnson, J.L.1    Rajagopalan, K.V.2
  • 36
    • 0025228504 scopus 로고
    • Molybdopterin guanine dinucleotide: A modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans
    • Johnson, J. L., Bastian, N. R. & Rajagopalan, K. V. (1990). Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans. Proc. Natl Acad. Sci. USA, 87, 3190-3194.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 3190-3194
    • Johnson, J.L.1    Bastian, N.R.2    Rajagopalan, K.V.3
  • 37
    • 0025804879 scopus 로고
    • Identification of a molybdopterin-containing molybdenum cofactor in xanthine dehydrogenase from Pseudomonas aeruginosa
    • Johnson, J. L., Chaudhury, M. & Rajagopalan, K. V. (1991a). Identification of a molybdopterin-containing molybdenum cofactor in xanthine dehydrogenase from Pseudomonas aeruginosa. BioFactors, 3, 103-107.
    • (1991) BioFactors , vol.3 , pp. 103-107
    • Johnson, J.L.1    Chaudhury, M.2    Rajagopalan, K.V.3
  • 38
    • 0025835008 scopus 로고
    • Molybdenum cofactor biosynthesis in Escherichia coli: Requirement of the chlb gene product for the formation of molybdopterin guanine dinucleotide
    • Johnson, J. L., Indermaur, L. W. & Rajagopalan, K. V. (1991b). Molybdenum cofactor biosynthesis in Escherichia coli: requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide. J. Biol. Chem. 266, 12140-12145.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12140-12145
    • Johnson, J.L.1    Indermaur, L.W.2    Rajagopalan, K.V.3
  • 39
    • 0000356656 scopus 로고
    • A graphics model building and refinement system for macromolecules
    • Jones, A. T. (1978). A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11, 268-272.
    • (1978) J. Appl. Crystallog. , vol.11 , pp. 268-272
    • Jones, A.T.1
  • 40
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, A. T., Zou, J.-Y., Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, A.T.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 41
    • 0017616853 scopus 로고
    • Effects of permeability barriers imposed by the cytoplasmic membrane
    • Jones, R. W. & Garland, P. B. (1977). Effects of permeability barriers imposed by the cytoplasmic membrane. Biochem. J. 164, 199-211.
    • (1977) Biochem. J. , vol.164 , pp. 199-211
    • Jones, R.W.1    Garland, P.B.2
  • 42
    • 0020997912 scopus 로고
    • Dictionary of secondary structures: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. & Sander, C. (1983). Dictionary of secondary structures: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers, 22, 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 44
    • 0026705527 scopus 로고
    • Structural models for the metal centres in the nitrogenase molybdenum-iron protein
    • Kim J. & Rees D. C. (1992a). Structural models for the metal centres in the nitrogenase molybdenum-iron protein. Science, 257, 1677-1682.
    • (1992) Science , vol.257 , pp. 1677-1682
    • Kim, J.1    Rees, D.C.2
  • 45
    • 0026734002 scopus 로고
    • Crystallographic structure and functional implication of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii
    • Kim J. & Rees D. C. (1992b). Crystallographic structure and functional implication of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii. Nature, 360, 553-560.
    • (1992) Nature , vol.360 , pp. 553-560
    • Kim, J.1    Rees, D.C.2
  • 46
    • 0030592480 scopus 로고    scopus 로고
    • Isolation, cloning, sequence analysis and localization of the operon encoding dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus
    • Knäblein, J., Mann, K., Ehlert, S., Fonstein, M., Huber, R. & Schneider, F. (1996). Isolation, cloning, sequence analysis and localization of the operon encoding dimethyl sulfoxide/trimethylamine N-oxide reductase from Rhodobacter capsulatus. J. Mol. Biol. 263, 40-52.
    • (1996) J. Mol. Biol. , vol.263 , pp. 40-52
    • Knäblein, J.1    Mann, K.2    Ehlert, S.3    Fonstein, M.4    Huber, R.5    Schneider, F.6
  • 47
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 48
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., McArthur, M. W., Moss, D. S. & Thronton, J. M. (1993). PROCHECK - a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thronton, J.M.4
  • 49
    • 0003195664 scopus 로고
    • Recent changes to the MOSFLM package for processing film and imageplate data
    • available from the Librarian, SERC Laboratory, Darresbury, Warrington WA4 4AD, UK
    • Leslie, A. G. W, (1991). Recent changes to the MOSFLM package for processing film and imageplate data. CCP4 and ESF-EACMB Newsletter on Protein Crystallography, available from the Librarian, SERC Laboratory, Darresbury, Warrington WA4 4AD, UK.
    • (1991) CCP4 and ESF-EACMB Newsletter on Protein Crystallography
    • Leslie, A.G.W.1
  • 50
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the Archeon T. acidophilum at 3.4 Å resolution
    • Löwe, J., Stock, D., Jap, B., Zwickel, P., Baumeister, W. & Huber, R. (1995). Crystal structure of the 20S proteasome from the Archeon T. acidophilum at 3.4 Å resolution. Science, 268, 533-539.
    • (1995) Science , vol.268 , pp. 533-539
    • Löwe, J.1    Stock, D.2    Jap, B.3    Zwickel, P.4    Baumeister, W.5    Huber, R.6
  • 51
    • 0014963075 scopus 로고
    • On the mechanism of inactivation of xanthine oxidase by cyanide
    • Massey, V. & Edmondson, D. E. (1970). On the mechanism of inactivation of xanthine oxidase by cyanide. J. Biol. Chem. 245, 6595-6598.
    • (1970) J. Biol. Chem. , vol.245 , pp. 6595-6598
    • Massey, V.1    Edmondson, D.E.2
  • 52
    • 0014432781 scopus 로고
    • Solvent contents of protein crystals
    • Matthews, B. W. (1968). Solvent contents of protein crystals. J. Mol. Biol. 33, 491-497.
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 53
    • 0028556393 scopus 로고
    • Photosynthetic electron transport and anaerobic metabolism in purple non-sulfur phototrophic bacteria
    • McEwan, A. G. (1994). Photosynthetic electron transport and anaerobic metabolism in purple non-sulfur phototrophic bacteria. Antonie van Leeuwenhoek, 66, 151-164.
    • (1994) Antonie van Leeuwenhoek , vol.66 , pp. 151-164
    • McEwan, A.G.1
  • 54
    • 0000355874 scopus 로고
    • Identification of cytochromes involved in electron transport to trimethylamine N-oxide/dimethylsulphoxide reductase in Rhodobacter capsulatus
    • McEwan, A. G., Richardson, D. J., Hudig, H., Ferguson, S. J. & Jackson, J. B. (1989). Identification of cytochromes involved in electron transport to trimethylamine N-oxide/dimethylsulphoxide reductase in Rhodobacter capsulatus. Biochim. Biophys. Acta, 973, 308-314.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 308-314
    • McEwan, A.G.1    Richardson, D.J.2    Hudig, H.3    Ferguson, S.J.4    Jackson, J.B.5
  • 55
    • 0026065682 scopus 로고
    • Purification and properties of the dimethyl sulfoxide reductase from Rhodobacter capsulatus
    • McEwan, A. G., Ferguson, S. J. & Jackson, J. B. (1991). Purification and properties of the dimethyl sulfoxide reductase from Rhodobacter capsulatus. Biochem. J. 274, 305-307.
    • (1991) Biochem. J. , vol.274 , pp. 305-307
    • McEwan, A.G.1    Ferguson, S.J.2    Jackson, J.B.3
  • 58
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A, 50, 157-163.
    • (1994) Acta Crystallog. Sect. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 59
    • 0000732609 scopus 로고
    • Grasp-graphical representation and analysis of surface properties
    • Nicholls, A., Bharadwaj, R. & Honig, B. (1993). Grasp-graphical representation and analysis of surface properties. Biophys. J. 64, A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 60
    • 0025304436 scopus 로고
    • Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in E. coli
    • Pierson, D. E. & Campbell, A. (1990). Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in E. coli. J. Bacteriol. 172, 2194-2198.
    • (1990) J. Bacteriol. , vol.172 , pp. 2194-2198
    • Pierson, D.E.1    Campbell, A.2
  • 61
    • 0028914525 scopus 로고
    • Molecular cloning and expression of biotin sulfoxide reductase from Rhodobacter sphaeroides forma sp. Denitrificans
    • Pollock, V. V. & Barber, M. J. (1995). Molecular cloning and expression of biotin sulfoxide reductase from Rhodobacter sphaeroides forma sp. Denitrificans. Arch. Biochem. 318, 322-332.
    • (1995) Arch. Biochem. , vol.318 , pp. 322-332
    • Pollock, V.V.1    Barber, M.J.2
  • 64
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
    • Schindelin, H., Kisker, C., Hilton, J., Rajagopalan, K. V. & Rees, D. C. (1996). Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. Science, 272, 1615-1621.
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1    Kisker, C.2    Hilton, J.3    Rajagopalan, K.V.4    Rees, D.C.5
  • 65
    • 0029159268 scopus 로고
    • Direct oxygen atom transfer in the mechanism of action of Rhodobacter sphaeroides dimethyl sulfoxide reductase
    • Schultz, B. E., Hille, R. & Holm, R. H. (1995). Direct oxygen atom transfer in the mechanism of action of Rhodobacter sphaeroides dimethyl sulfoxide reductase. J. Am. Chem. Soc. 117, 827-828.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 827-828
    • Schultz, B.E.1    Hille, R.2    Holm, R.H.3
  • 66
    • 0011871845 scopus 로고
    • Moras, D., Podjarini, A. D. & Thierry, J. C., eds, Oxford University Press, Oxford
    • Steigemann, W. (1991). In From Chemistry to Biology (Moras, D., Podjarini, A. D. & Thierry, J. C., eds), vol. 5, pp. 115-125, Oxford University Press, Oxford.
    • (1991) From Chemistry to Biology , vol.5 , pp. 115-125
    • Steigemann, W.1
  • 67
    • 0000260891 scopus 로고
    • MOPAC: A general molecular orbital package (version 6.0)
    • F. J. Seiler Res. Lab., US Air Force Academy, CO 80843
    • Stewart, J. J. P. (1990). MOPAC: a general molecular orbital package (version 6.0). QCPE-Program Nr. 455. F. J. Seiler Res. Lab., US Air Force Academy, CO 80843.
    • (1990) QCPE-Program Nr. , vol.455
    • Stewart, J.J.P.1
  • 68
    • 85030290362 scopus 로고    scopus 로고
    • SYBYL (1995). Version 6.2, Tripos, Inc., 1699 S. Hanley Road, St. Louis, MO 63144-2913
    • SYBYL (1995). Version 6.2, Tripos, Inc., 1699 S. Hanley Road, St. Louis, MO 63144-2913.
  • 70
    • 0023268434 scopus 로고
    • The molybdenum iron-sulfur protein from Desulfovibrio gigas as a form of aldehyde oxidase
    • Turner, N., Barata, B., Bray, R. C., Deistung, J., LeGall, J. & Moura, J. J. G. (1987). The molybdenum iron-sulfur protein from Desulfovibrio gigas as a form of aldehyde oxidase. Biochem. J. 243, 755-761.
    • (1987) Biochem. J. , vol.243 , pp. 755-761
    • Turner, N.1    Barata, B.2    Bray, R.C.3    Deistung, J.4    LeGall, J.5    Moura, J.J.G.6
  • 71
    • 0024309237 scopus 로고
    • Information from EXAFS spectroscopy on the structures of different froms of the molybdenum in xanthine oxidase and the catalytic mechanism of the enzyme
    • Turner, N., Bray, R. C. & Diakun, G. P. (1989). Information from EXAFS spectroscopy on the structures of different froms of the molybdenum in xanthine oxidase and the catalytic mechanism of the enzyme. Biochem. J. 260, 563-571.
    • (1989) Biochem. J. , vol.260 , pp. 563-571
    • Turner, N.1    Bray, R.C.2    Diakun, G.P.3
  • 72
    • 0019875878 scopus 로고
    • The redox potential for dimethyl sulfoxide reduction to dimethyl sulphide
    • Wood, P. M. (1981). The redox potential for dimethyl sulfoxide reduction to dimethyl sulphide. FEBS Letters, 124, 11-14.
    • (1981) FEBS Letters , vol.124 , pp. 11-14
    • Wood, P.M.1
  • 73
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum and possible cofactor binding domains
    • Wooton, J. C., Nicolson, R. E., Cock J. M., Walters, D. E., Bruke, J. F., Doyle, W. A. & Bray, R. C. (1991). Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor binding domains. Biochim. Biophys. Acta, 1057, 157-185.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 157-185
    • Wooton, J.C.1    Nicolson, R.E.2    Cock, J.M.3    Walters, D.E.4    Bruke, J.F.5    Doyle, W.A.6    Bray, R.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.