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Volumn 5, Issue 5, 1997, Pages 691-699

Crystal structure of nitrile hydratase reveals a novel iron centre in a novel fold

Author keywords

iron centre; metalloenzyme; nitrile hydratase; non heme iron; protein crystallography

Indexed keywords


EID: 0031570299     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00223-2     Document Type: Article
Times cited : (294)

References (41)
  • 1
    • 0030250538 scopus 로고    scopus 로고
    • Nitrile hydratase and its application to industrial production of acrylamide
    • Yamada, H. & Kobayashi, M. (1996). Nitrile hydratase and its application to industrial production of acrylamide. Biosci. Biotechol. Biochem. 60, 1391-1400
    • (1996) Biosci. Biotechol. Biochem. , vol.60 , pp. 1391-1400
    • Yamada, H.1    Kobayashi, M.2
  • 2
    • 0029102389 scopus 로고
    • Microbial degradation of acrylonitrile waste effluents: The degradation of effluents and condensates from the manufacture of acrylonitrile
    • Wyatt, J.M. & Knowles, C.J. (1995). Microbial degradation of acrylonitrile waste effluents: the degradation of effluents and condensates from the manufacture of acrylonitrile. Int. Biodeter. Biodegrad. 35, 227-248
    • (1995) Int. Biodeter. Biodegrad. , vol.35 , pp. 227-248
    • Wyatt, J.M.1    Knowles, C.J.2
  • 3
    • 0030452421 scopus 로고    scopus 로고
    • Resonance Raman evidence that photodissociation of nitric oxide from the non-heme iron center activates nitrile hydratase from Rhodococcussp. N-771
    • Noguchi, T., Hoshino, M., Tsujimura, M., Odaka, M., Inoue, Y. & Endo, I. (1996). Resonance Raman evidence that photodissociation of nitric oxide from the non-heme iron center activates nitrile hydratase from Rhodococcussp. N-771. Biochemistry 35, 16777-16781
    • (1996) Biochemistry , vol.35 , pp. 16777-16781
    • Noguchi, T.1    Hoshino, M.2    Tsujimura, M.3    Odaka, M.4    Inoue, Y.5    Endo, I.6
  • 4
    • 0026480892 scopus 로고
    • Enzymatic synthesis of acrylamide: A success story not over yet
    • Kobayashi, M., Nagasawa, T. & Yamada, H. (1992). Enzymatic synthesis of acrylamide: a success story not over yet. Trends Biotechnol. 10, 402-408
    • (1992) Trends Biotechnol. , vol.10 , pp. 402-408
    • Kobayashi, M.1    Nagasawa, T.2    Yamada, H.3
  • 5
    • 0029962401 scopus 로고    scopus 로고
    • Photoreactive nitrile hydratase: The photoreaction site is located on the alpha subunit
    • Tsujimura, M., Okada, M., Nagashima, S., Yohda, M. & Endo, I. (1996). Photoreactive nitrile hydratase: the photoreaction site is located on the alpha subunit. J. Biochem. 119, 407-413
    • (1996) J. Biochem. , vol.119 , pp. 407-413
    • Tsujimura, M.1    Okada, M.2    Nagashima, S.3    Yohda, M.4    Endo, I.5
  • 6
    • 0023229582 scopus 로고
    • The first non-heme iron enzyme with a typical low-spin iron(III)-active center
    • Sugiura, Y., Kuwahara, J., Nagasawa, T. & Yamada, H. (1987). The first non-heme iron enzyme with a typical low-spin iron(III)-active center. J. Am. Chem. Soc. 109, 5848-5850
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 5848-5850
    • Sugiura, Y.1    Kuwahara, J.2    Nagasawa, T.3    Yamada, H.4
  • 7
    • 0011041731 scopus 로고
    • An active site model of nitrile hydratase: Axially coordinate non-heme complexes in the lowspin ferric state
    • Sakurai, H., Tsuchiya, K. & Migita, K. (1988). An active site model of nitrile hydratase: axially coordinate non-heme complexes in the lowspin ferric state, Inorg. Chem. 27, 3877-3879
    • (1988) Inorg. Chem. , vol.27 , pp. 3877-3879
    • Sakurai, H.1    Tsuchiya, K.2    Migita, K.3
  • 9
    • 0030013684 scopus 로고    scopus 로고
    • An implicit TRIPLE effect in mims pulsed ENDOR: A sensitive new technique for determining signs of hyperfine couplings
    • Doan, P.E., Nelson, M.J., Jin, H. & Hoffman, B.M. (1996). An implicit TRIPLE effect in mims pulsed ENDOR: a sensitive new technique for determining signs of hyperfine couplings. J. Am. Chem. Soc. 118, 7014-7015
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7014-7015
    • Doan, P.E.1    Nelson, M.J.2    Jin, H.3    Hoffman, B.M.4
  • 10
    • 0000841421 scopus 로고
    • A novel iron-sulfur center in nitrile hydratase from Brevibacterium sp.
    • Nelson, M.J., et al., & Que, L. Jr. (1991). A novel iron-sulfur center in nitrile hydratase from Brevibacterium sp. J. Am. Chem. Soc. 113, 7072-7073
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7072-7073
    • Nelson, M.J.1    Que Jr., L.2
  • 11
    • 0029758880 scopus 로고    scopus 로고
    • X-ray spectroscopy of nitrile hydratase at pH7 and 9
    • Scarrow, R.C., et al., & Nelson, M.J. (1996). X-ray spectroscopy of nitrile hydratase at pH7 and 9. Biochemistry 35, 10078-10088
    • (1996) Biochemistry , vol.35 , pp. 10078-10088
    • Scarrow, R.C.1    Nelson, M.J.2
  • 12
    • 0029738645 scopus 로고    scopus 로고
    • Resonance Raman spectroscopy of nitrile hydratase, a novel iron-sulfur enzyme
    • Brennan, B.A., Cummings, J.G., Chase, D.B., Turner, I.M. Jr. & Nelson, M.J. (1996). Resonance Raman spectroscopy of nitrile hydratase, a novel iron-sulfur enzyme. Biochemistry 35, 10068-10077
    • (1996) Biochemistry , vol.35 , pp. 10068-10077
    • Brennan, B.A.1    Cummings, J.G.2    Chase, D.B.3    Turner Jr., I.M.4    Nelson, M.J.5
  • 13
    • 84889120137 scopus 로고
    • Improved methods for building protein models into electron-density maps and the location of errors in these models
    • Jones, T.A., Zou J.-Y., Cowan, S. & Kjeldgaard, M. (1991). Improved methods for building protein models into electron-density maps and the location of errors in these models. Acta Cryst. A 47, 100-119
    • (1991) Acta Cryst. A , vol.47 , pp. 100-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 14
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a thermostable protein from the archeon Sulfolobus sulfataricus
    • Baumann, H., Knapp, S., Lundbäck, T., Ladenstein, R. & Hard, T. (1994). Solution structure and DNA-binding properties of a thermostable protein from the archeon Sulfolobus sulfataricus. Nat. Struct. Biol. 1, 808-819
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 808-819
    • Baumann, H.1    Knapp, S.2    Lundbäck, T.3    Ladenstein, R.4    Hard, T.5
  • 15
    • 0023193446 scopus 로고
    • The accessible surface area and stability of oligomeric proteins
    • Miller, S., Lesk, A.M., Janin, J. & Chothia, C. (1987). The accessible surface area and stability of oligomeric proteins. Nature 328, 834-836
    • (1987) Nature , vol.328 , pp. 834-836
    • Miller, S.1    Lesk, A.M.2    Janin, J.3    Chothia, C.4
  • 16
    • 0023059799 scopus 로고
    • Nitrile hydratase from Brevibacterium R312: Purification and characterization
    • Nagasawa, T., Ryuno, K. & Yamada, H. (1986). Nitrile hydratase from Brevibacterium R312: purification and characterization. Biochem. Biophys. Res. Commun. 139, 1305-1312
    • (1986) Biochem. Biophys. Res. Commun. , vol.139 , pp. 1305-1312
    • Nagasawa, T.1    Ryuno, K.2    Yamada, H.3
  • 17
    • 0025306731 scopus 로고
    • Purification of inactivated photoresponsive nitrile hydratase
    • Nagamune, T., et al., & Endo, I. (1990). Purification of inactivated photoresponsive nitrile hydratase. Biochem. Biophys. Res. Commun. 168, 437-442
    • (1990) Biochem. Biophys. Res. Commun. , vol.168 , pp. 437-442
    • Nagamune, T.1    Endo, I.2
  • 18
    • 0030941934 scopus 로고    scopus 로고
    • A stereoselective cobalt-containing nitrile hydratase
    • in press
    • Payne, M.S., et al., & Nelson, M.J. (1997). A stereoselective cobalt-containing nitrile hydratase. Biochemistry, in press.
    • (1997) Biochemistry
    • Payne, M.S.1    Nelson, M.J.2
  • 20
    • 0029805756 scopus 로고    scopus 로고
    • Nitrile hydratase from Rhodococcus rhodochrous J1 contains a non-corrinoid cobalt with two sulfur ligands
    • Brennan, B.A., Alms, G., Nelson, M.J., Durney, L.T. & Scarrow, R.C. (1996). Nitrile hydratase from Rhodococcus rhodochrous J1 contains a non-corrinoid cobalt with two sulfur ligands. J. Am. Chem. Soc. 118, 9194-9195
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 9194-9195
    • Brennan, B.A.1    Alms, G.2    Nelson, M.J.3    Durney, L.T.4    Scarrow, R.C.5
  • 21
    • 0001735877 scopus 로고
    • Nitrile hydratase-catalyzed production of nicotinamide from 3-cyanopyridine in Rhodococcus rhodochrous J1
    • Nagasawa, T., Mathew, C.D., Mauger, J. & Yamada, H. (1988). Nitrile hydratase-catalyzed production of nicotinamide from 3-cyanopyridine in Rhodococcus rhodochrous J1. Appl. Environ. Microbiol. 1766-1769
    • (1988) Appl. Environ. Microbiol. , pp. 1766-1769
    • Nagasawa, T.1    Mathew, C.D.2    Mauger, J.3    Yamada, H.4
  • 22
    • 0024299530 scopus 로고
    • Significant interaction between the low-spin iron (II) site and pyrroloquinoline quinone in the active center of nitrile hydratase
    • Sugiura, Y., Kuwahara, J., Nagasawa, T. & Yamada, H. (1988). Significant interaction between the low-spin iron (II) site and pyrroloquinoline quinone in the active center of nitrile hydratase. Biochem. Biophys. Res. Commun. 154, 522-528
    • (1988) Biochem. Biophys. Res. Commun. , vol.154 , pp. 522-528
    • Sugiura, Y.1    Kuwahara, J.2    Nagasawa, T.3    Yamada, H.4
  • 23
    • 0029797384 scopus 로고    scopus 로고
    • Key role of alkanoic acids on the spectral properties, activity, and activesite stability of iron-containing nitrile hydratase from Brevibacterium R312
    • Kopf, M.A., Bonnet, D., Artaud, I., Petre, D. & Mansuy, D. (1996). Key role of alkanoic acids on the spectral properties, activity, and activesite stability of iron-containing nitrile hydratase from Brevibacterium R312. Eur. J. Biochem. 240, 239-244
    • (1996) Eur. J. Biochem. , vol.240 , pp. 239-244
    • Kopf, M.A.1    Bonnet, D.2    Artaud, I.3    Petre, D.4    Mansuy, D.5
  • 24
    • 0000269767 scopus 로고
    • Synthesis and base hydrolysis of pentammine N,N-dimethylformamide and acetonitrile complexes of Rh(III) and Ir(III)
    • Curtis, N.J. & Sargeson, A.M. (1984). Synthesis and base hydrolysis of pentammine N,N-dimethylformamide and acetonitrile complexes of Rh(III) and Ir(III). J. Am. Chem. Soc. 106, 625-630
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 625-630
    • Curtis, N.J.1    Sargeson, A.M.2
  • 25
    • 0030049613 scopus 로고    scopus 로고
    • Cytidine deaminase complexed to 3-deazacytidine: A 'valence buffer' in zinc enzyme catalysis
    • Xiang, S., Short, S.A., Wolfenden, R. & Carter, C.W. Jr. (1996). Cytidine deaminase complexed to 3-deazacytidine: a 'valence buffer' in zinc enzyme catalysis. Biochemistry 35, 1335-1341
    • (1996) Biochemistry , vol.35 , pp. 1335-1341
    • Xiang, S.1    Short, S.A.2    Wolfenden, R.3    Carter Jr., C.W.4
  • 26
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • (Sawyer, L., Isaacs, N. & Bailey, S.S., eds) SERC Daresbury Laboratory, Warrington, UK
    • Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data collection and processing. (Sawyer, L., Isaacs, N. & Bailey, S.S., eds) pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
    • (1993) Proceedings of the CCP4 Study Weekend: Data Collection and Processing , pp. 56-62
    • Otwinowski, Z.1
  • 27
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project No4. (1994). The CCP4 suite: programs for protein crystallography. Acta Cryst. D 50, 760-763
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 28
    • 0000858864 scopus 로고
    • SQUASH: Combining constraints for macromolecular phase refinement and extension
    • Zhang, K.Y. (1993). SQUASH: combining constraints for macromolecular phase refinement and extension. Acta Cryst. D 49, 213-222
    • (1993) Acta Cryst. D , vol.49 , pp. 213-222
    • Zhang, K.Y.1
  • 29
  • 30
    • 0026013697 scopus 로고
    • Cloning and characterisation of an amidase gene from Rhodococcus species N-774 and its expression in Escherichia coli
    • Hashimoto, Y., Nishiyama, M., Ikehata, O., Horinouchi, S. & Beppu, T. (1991). Cloning and characterisation of an amidase gene from Rhodococcus species N-774 and its expression in Escherichia coli. Biochim. Biophys. Acta 1088, 225-233
    • (1991) Biochim. Biophys. Acta , vol.1088 , pp. 225-233
    • Hashimoto, Y.1    Nishiyama, M.2    Ikehata, O.3    Horinouchi, S.4    Beppu, T.5
  • 31
    • 0025604503 scopus 로고
    • Purification, cloning and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: Structural evidence for a conserved gene coupling with nitrile hydratase
    • Mayaux, J.-F., Cerbelaud, E., Soubrier, F., Faucher, D. & Petre, D. (1990). Purification, cloning and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for a conserved gene coupling with nitrile hydratase J. Bacteriol. 172, 6764-6773
    • (1990) J. Bacteriol. , vol.172 , pp. 6764-6773
    • Mayaux, J.-F.1    Cerbelaud, E.2    Soubrier, F.3    Faucher, D.4    Petre, D.5
  • 32
    • 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 235, 458-460
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 33
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structure
    • Brünger, A.T. (1992). Free R-value: a novel statistical quantity for assessing the accuracy of crystal structure. Nature 355, 472-475
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 34
    • 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 Cryst. A 47, 392-400
    • (1991) Acta Cryst. A , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 36
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). Molscript: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 37
    • 0028057108 scopus 로고
    • Raster 3D version 2.0: A program for photorealistic molecular graphics
    • Merrit, E.A. & Murphy, M.E.P. (1994). Raster 3D version 2.0: a program for photorealistic molecular graphics. Acta Cryst. D 50, 869-873
    • (1994) Acta Cryst. D , vol.50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 38
    • 0027651143 scopus 로고
    • Characterisation of nitrile hydratase genes cloned by DNA screening from Rhodococcus erythropolis
    • Duran, R., Nishiyama, M., Horinouchi, S. & Beppu, T. (1993). Characterisation of nitrile hydratase genes cloned by DNA screening from Rhodococcus erythropolis. Biosci. Biotechol. Biochem. 57, 1323-1328
    • (1993) Biosci. Biotechol. Biochem. , vol.57 , pp. 1323-1328
    • Duran, R.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 39
    • 0025761763 scopus 로고
    • Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chloraphis B23
    • Nishiyama, M., Horinouchi, S., Kobayashi, M., Nagasawa, T., Yamada, T. & Beppu, T. (1991). Cloning and characterization of genes responsible for metabolism of nitrile compounds from Pseudomonas chloraphis B23. J. Bacteriol. 173, 2465-2472
    • (1991) J. Bacteriol. , vol.173 , pp. 2465-2472
    • Nishiyama, M.1    Horinouchi, S.2    Kobayashi, M.3    Nagasawa, T.4    Yamada, T.5    Beppu, T.6
  • 40
    • 0025747960 scopus 로고
    • Purification, cloning and primary structure of an enantiomer-selective amidase from a Rhodococcus strain: Structural evidence for a conserved gene coupling with nitrile hydratase
    • Mayaux, J.-F., Cerbelaud, E., Soubrier, F., Yeh, P., Blanche, F. & Petre, D. (1991). Purification, cloning and primary structure of an enantiomer-selective amidase from a Rhodococcus strain: structural evidence for a conserved gene coupling with nitrile hydratase. J. Bacteriol. 173, 6694-6704
    • (1991) J. Bacteriol. , vol.173 , pp. 6694-6704
    • Mayaux, J.-F.1    Cerbelaud, E.2    Soubrier, F.3    Yeh, P.4    Blanche, F.5    Petre, D.6
  • 41
    • 0025934442 scopus 로고
    • Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1
    • Kobayashi, M., Nishiyama, M., Nagasawa, T., Horinouchi, S., Beppu, T. & Yamada, H. (1991). Cloning, nucleotide sequence and expression in Escherichia coli of two cobalt-containing nitrile hydratase genes from Rhodococcus rhodochrous J1. Biochim. Biophys. Acta 1129, 23-33
    • (1991) Biochim. Biophys. Acta , vol.1129 , pp. 23-33
    • Kobayashi, M.1    Nishiyama, M.2    Nagasawa, T.3    Horinouchi, S.4    Beppu, T.5    Yamada, H.6


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