-
1
-
-
0021116476
-
Saturation behavior of the manganese-containing superoxide dismutase from Paracoccus denitrificans
-
1. Terech, A., Pucheault, J. & Ferradini, C. (1983) Saturation behavior of the manganese-containing superoxide dismutase from Paracoccus denitrificans. Biochem. Biophys. Res. Commun. 113, 114-120.
-
(1983)
Biochem. Biophys. Res. Commun.
, vol.113
, pp. 114-120
-
-
Terech, A.1
Pucheault, J.2
Ferradini, C.3
-
2
-
-
0000348087
-
Steady states kinetic studies of superoxide dismutases: Properties of the iron containing protein from Escherichia coli
-
2. Bull, C. & Fee, J.A. (1985) Steady states kinetic studies of superoxide dismutases: properties of the iron containing protein from Escherichia coli. J. Am. Chem. Soc. 107, 3295-3304.
-
(1985)
J. Am. Chem. Soc.
, vol.107
, pp. 3295-3304
-
-
Bull, C.1
Fee, J.A.2
-
3
-
-
0032522349
-
pH dependent inhibition by azide and fluoride of the iron superoxide dismutase from Propionibacterium shermanii
-
3. Meier, B., Scherk, C., Schmidt, M. & Parak, F. (1998) pH dependent inhibition by azide and fluoride of the iron superoxide dismutase from Propionibacterium shermanii. Biochem. J. 331, 403-407.
-
(1998)
Biochem. J.
, vol.331
, pp. 403-407
-
-
Meier, B.1
Scherk, C.2
Schmidt, M.3
Parak, F.4
-
4
-
-
0028852868
-
The pH-dependent changes of the enzymic activity and spectroscopic properties of iron-substituted manganese superoxide dismutase
-
4. Yamakura, F., Kobayashi, K., Harumi, U.E. & Konno, M. (1995) The pH-dependent changes of the enzymic activity and spectroscopic properties of iron-substituted manganese superoxide dismutase. Eur. J. Biochem. 227, 700-706.
-
(1995)
Eur. J. Biochem.
, vol.227
, pp. 700-706
-
-
Yamakura, F.1
Kobayashi, K.2
Harumi, U.E.3
Konno, M.4
-
5
-
-
0028938504
-
X-ray absorption spectroscopy on the iron site in E. coli Fe (III) superoxide dismutase
-
5. Tierney, D.L., Fee, J.A., Ludwig, M.L. & Penner-Hahn, J.E. (1995) X-ray absorption spectroscopy on the iron site in E. coli Fe (III) superoxide dismutase. Biochemistry 34, 1661-1668.
-
(1995)
Biochemistry
, vol.34
, pp. 1661-1668
-
-
Tierney, D.L.1
Fee, J.A.2
Ludwig, M.L.3
Penner-Hahn, J.E.4
-
6
-
-
0013600361
-
The active center of superoxide dismutase from Propionibacterium shermanii
-
6. Iakovleva, O., Parak, F., Rimke, T., Meier, B., Hüttermann, J. & Kappl, R. (1996) The active center of superoxide dismutase from Propionibacterium shermanii. II Nuovo Cimento 18, 199-212.
-
(1996)
II Nuovo Cimento
, vol.18
, pp. 199-212
-
-
Iakovleva, O.1
Parak, F.2
Rimke, T.3
Meier, B.4
Hüttermann, J.5
Kappl, R.6
-
7
-
-
0029997688
-
EXAFS investigations of the active site of iron superoxide dismutase of Escherichia coli and Propionibacterium shermanii
-
7. Scherk, C., Schmidt, M., Nolting, H.F., Meier, B. & Parak, F. (1996) EXAFS investigations of the active site of iron superoxide dismutase of Escherichia coli and Propionibacterium shermanii. J. Eur. Biophys. 24, 243-250.
-
(1996)
J. Eur. Biophys.
, vol.24
, pp. 243-250
-
-
Scherk, C.1
Schmidt, M.2
Nolting, H.F.3
Meier, B.4
Parak, F.5
-
8
-
-
0028933323
-
Structure-function in Escherichia coli iron superoxide dismutase: Comparisons with manganese enzyme from Thermus thermophilus
-
8. Lah, M.S., Dixon, M.M., Pattridge, K.A., Stallings, W.C., Fee, J.A. & Ludwig, M.L. (1995) Structure-function in Escherichia coli iron superoxide dismutase: comparisons with manganese enzyme from Thermus thermophilus. Biochemistry 34, 1646-1660.
-
(1995)
Biochemistry
, vol.34
, pp. 1646-1660
-
-
Lah, M.S.1
Dixon, M.M.2
Pattridge, K.A.3
Stallings, W.C.4
Fee, J.A.5
Ludwig, M.L.6
-
9
-
-
0001122503
-
X-ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or Mn
-
9. Schmidt, M., Meier, B. & Parak, F. (1996) X-ray structure of the cambialistic superoxide dismutase from Propionibacterium shermanii active with Fe or Mn. J. Biol. Inorg. Chem. 1, 532-541.
-
(1996)
J. Biol. Inorg. Chem.
, vol.1
, pp. 532-541
-
-
Schmidt, M.1
Meier, B.2
Parak, F.3
-
10
-
-
0028103275
-
CCP4, collaborative computational project, number 4
-
10. CCP4 (1994) CCP4, Collaborative computational project, number 4 Acta Crystallogr. D50, 760-763.
-
(1994)
Acta Crystallogr.
, vol.D50
, pp. 760-763
-
-
-
11
-
-
0026597444
-
The free R-value: A novel statistical quality for assessing the accuracy of crystal structures
-
11. Brünger, A.T. (1992) The free R-value: a novel statistical quality for assessing the accuracy of crystal structures. Nature 335, 472-474.
-
(1992)
Nature
, vol.335
, pp. 472-474
-
-
Brünger, A.T.1
-
13
-
-
84920325457
-
AMoRe: An automated package for molecular replacement
-
13. Navaza, J. (1994) AMoRe: an automated package for molecular replacement. Acta Crystallogr. A50, 157-163.
-
(1994)
Acta Crystallogr.
, vol.A50
, pp. 157-163
-
-
Navaza, J.1
-
14
-
-
84944812409
-
Improved Fourier coefficients for maps using phases from partial structures with errors
-
14. Read, R.J. (1986) Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallogr. A42, 140-149.
-
(1986)
Acta Crystallogr.
, vol.A42
, pp. 140-149
-
-
Read, R.J.1
-
15
-
-
0002215568
-
The structure of the azide coordinated superoxide dismutase of Propionibacterium shermanii investigated by X-ray structure analysis, extended X-ray absorption fine structure, Mössbauer and electron paramagnetic resonance spectroscopy
-
15. Schmidt, M., Scherk, C., Iakovleva, O., Nolting, H.F., Meier, B. & Parak, F. (1998) The structure of the azide coordinated superoxide dismutase of Propionibacterium shermanii investigated by X-ray structure analysis, extended X-ray absorption fine structure, Mössbauer and electron paramagnetic resonance spectroscopy. Inorganica Chimica Acta 275-276, 65-72.
-
(1998)
Inorganica Chimica Acta
, vol.275-276
, pp. 65-72
-
-
Schmidt, M.1
Scherk, C.2
Iakovleva, O.3
Nolting, H.F.4
Meier, B.5
Parak, F.6
-
16
-
-
0020356135
-
Synthesis of either Fe-or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied
-
16. Meier, B., Barra, D., Bossa, F., Calabrese, L. & Rotilio, G. (1982) Synthesis of either Fe-or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied. J. Biol. Chem. 257, 13977-13980.
-
(1982)
J. Biol. Chem.
, vol.257
, pp. 13977-13980
-
-
Meier, B.1
Barra, D.2
Bossa, F.3
Calabrese, L.4
Rotilio, G.5
-
17
-
-
0023030627
-
A Streptococcus mutans superoxide dismutase that is active with either manganese or ion as a cofactor
-
17. Martin, M.E., Byers, B.R., Olson, M.O.J., Salin, M.L., Arceneaux, J.E.L. & Tolbert, C. (1986) A Streptococcus mutans superoxide dismutase that is active with either manganese or ion as a cofactor. J. Biol. Chem. 261, 9361-9367.
-
(1986)
J. Biol. Chem.
, vol.261
, pp. 9361-9367
-
-
Martin, M.E.1
Byers, B.R.2
Olson, M.O.J.3
Salin, M.L.4
Arceneaux, J.E.L.5
Tolbert, C.6
-
18
-
-
84889120137
-
Improved methods for building protein models in electron density maps and the location of errors in these models
-
18. Jones, A., Zou, J.Y., Couran, S.W. & Kielgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
-
(1991)
Acta Crystallogr.
, vol.A47
, pp. 110-119
-
-
Jones, A.1
Zou, J.Y.2
Couran, S.W.3
Kielgaard, M.4
-
19
-
-
0029944136
-
Low-temperature thermodicroismus marks a change in coordination for the metal ion in manganese superoxide dismutase
-
19. Whittaker, M.M. & Whittaker, J.M. (1996) Low-temperature thermodicroismus marks a change in coordination for the metal ion in manganese superoxide dismutase. Biochemistry 35, 6762-6770.
-
(1996)
Biochemistry
, vol.35
, pp. 6762-6770
-
-
Whittaker, M.M.1
Whittaker, J.M.2
-
20
-
-
0030888269
-
The conserved residue tyrosine 34 is essential for maximal activity of iron-superoxide dismutase from Escherichia coli
-
20. Hunter, T., Ikebukuro, K., Bannister, W.H., Bannister, J.V. & Hunter, G.J. (1997) The conserved residue tyrosine 34 is essential for maximal activity of iron-superoxide dismutase from Escherichia coli. Biochemistry 36, 4925-4933.
-
(1997)
Biochemistry
, vol.36
, pp. 4925-4933
-
-
Hunter, T.1
Ikebukuro, K.2
Bannister, W.H.3
Bannister, J.V.4
Hunter, G.J.5
-
21
-
-
0032492710
-
Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34
-
21. Guan, Y., Hickey, M.J., Borgstahl, G.E.O., Hallewell, R.A., Lepock, J.R., O'Connor, D., Hsieh, Y., Nick, H.S., Silverman, D.N. & Tainer, J.A. (1998) Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34. Biochemistry 37, 4722-4730.
-
(1998)
Biochemistry
, vol.37
, pp. 4722-4730
-
-
Guan, Y.1
Hickey, M.J.2
Borgstahl, G.E.O.3
Hallewell, R.A.4
Lepock, J.R.5
O'Connor, D.6
Hsieh, Y.7
Nick, H.S.8
Silverman, D.N.9
Tainer, J.A.10
-
23
-
-
0000755267
-
Kinetic studies of superoxide dismutases: Properties of the manganese-containing protein from Thermus thermophilus
-
23. Bull, C., Niederhofer, E.C., Yoshida, T. & Fee, J.A. (1991) Kinetic studies of superoxide dismutases: properties of the manganese-containing protein from Thermus thermophilus. J. Am. Chem. Soc. 113, 4069-4076.
-
(1991)
J. Am. Chem. Soc.
, vol.113
, pp. 4069-4076
-
-
Bull, C.1
Niederhofer, E.C.2
Yoshida, T.3
Fee, J.A.4
-
24
-
-
0032560945
-
Distinct metal environment in Fe-substituted manganese superoxide dismutase provides a structural basis of metal specifity
-
24. Edward, R.A., Whittaker, M.M., Jameson, G.B. & Baker, E.N. (1998) Distinct metal environment in Fe-substituted manganese superoxide dismutase provides a structural basis of metal specifity. J. Am. Chem. Soc. 120, 9684-9685.
-
(1998)
J. Am. Chem. Soc.
, vol.120
, pp. 9684-9685
-
-
Edward, R.A.1
Whittaker, M.M.2
Jameson, G.B.3
Baker, E.N.4
|