-
7
-
-
0028807552
-
-
Romao, M. J.; Archer, M.; Moura, I.; Moura, J. J. G.; LeGall, J.; Ensh, R.; Schneider, M.; Hof, P.: Huber, R. Science 1995, 270, 1170-1176.
-
(1995)
Science
, vol.270
, pp. 1170-1176
-
-
Romao, M.J.1
Archer, M.2
Moura, I.3
Moura, J.J.G.4
LeGall, J.5
Ensh, R.6
Schneider, M.7
Hof, P.8
Huber, R.9
-
8
-
-
0026086008
-
-
Bastian, N. R.; Kay, C. J.; Barber, M. J.; Rajasopalan, K. V. J. Biol. Chem. 1991, 266, 45-51.
-
(1991)
J. Biol. Chem.
, vol.266
, pp. 45-51
-
-
Bastian, N.R.1
Kay, C.J.2
Barber, M.J.3
Rajasopalan, K.V.4
-
9
-
-
0026065682
-
-
McEwan, A. G.; Ferguson, S. J.; Jackson, J. B. Biochem. J. 1991, 274, 305-307.
-
(1991)
Biochem. J.
, vol.274
, pp. 305-307
-
-
McEwan, A.G.1
Ferguson, S.J.2
Jackson, J.B.3
-
11
-
-
0025228504
-
-
Johnson, J. L.; Bastian, N. R.; Rajagopalan, K. V. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 3190-3194.
-
(1990)
Proc. Natl. Acad. Sci. U.S.A.
, vol.87
, pp. 3190-3194
-
-
Johnson, J.L.1
Bastian, N.R.2
Rajagopalan, K.V.3
-
12
-
-
13344274319
-
-
Bennet, B.; Benson, N.; McEwan, A. G.; Bray. R. C. Biochem. J. 1994.255, 321-331.
-
(1994)
Biochem. J.
, vol.255
, pp. 321-331
-
-
Bennet, B.1
Benson, N.2
McEwan, A.G.3
Bray, R.C.4
-
13
-
-
0026719264
-
-
Benson, N.: Farrar, J. A.: McEwan, A. G.; Thomson, A. J. FEBS Len. 1992, 307, 169-172.
-
(1992)
FEBS Len.
, vol.307
, pp. 169-172
-
-
Benson, N.1
Farrar, J.A.2
McEwan, A.G.3
Thomson, A.J.4
-
14
-
-
0001226830
-
-
Finnegan, M. G.; Hilton, J.; Rajagopalan, K. V.; Johnson, M. K. Inorg. Chem. 1993, 32, 2616-2617.
-
(1993)
Inorg. Chem.
, vol.32
, pp. 2616-2617
-
-
Finnegan, M.G.1
Hilton, J.2
Rajagopalan, K.V.3
Johnson, M.K.4
-
15
-
-
0025087286
-
-
Gruber, S.: Kilpatrick, L.; Bastian, N. R.; Rajogopalan, K. V.; Spiro, T. G. J. Am. Chem. Soc. 1990, 112, 8179-8180.
-
(1990)
J. Am. Chem. Soc.
, vol.112
, pp. 8179-8180
-
-
Gruber, S.1
Kilpatrick, L.2
Bastian, N.R.3
Rajogopalan, K.V.4
Spiro, T.G.5
-
16
-
-
0028912409
-
-
Kilpatrick, L.; Rajagopalan, K. V.; Hilton. J.; Bastian, N. R.; Steifel, E. I.; Pilato, R. S.; Spiro, T. G. Biochemistry 1995, 34, 3032-3039.
-
(1995)
Biochemistry
, vol.34
, pp. 3032-3039
-
-
Kilpatrick, L.1
Rajagopalan, K.V.2
Hilton, J.3
Bastian, N.R.4
Steifel, E.I.5
Pilato, R.S.6
Spiro, T.G.7
-
18
-
-
0023761568
-
-
George, G. N.; Prince, R. C.; Kipke, C. A.; Sunde. R. A.; Enemark, J. E. Biochem. J. 1988, 256, 307-309.
-
(1988)
Biochem. J.
, vol.256
, pp. 307-309
-
-
George, G.N.1
Prince, R.C.2
Kipke, C.A.3
Sunde, R.A.4
Enemark, J.E.5
-
19
-
-
0023325538
-
-
Cramer, S. P.; Tench, O.; Yocum, M.; George, G. N. Nucl. Instrum. Methods Phys. Res. 1988, A266, 586-591.
-
(1988)
Nucl. Instrum. Methods Phys. Res.
, vol.A266
, pp. 586-591
-
-
Cramer, S.P.1
Tench, O.2
Yocum, M.3
George, G.N.4
-
20
-
-
13344258355
-
-
note
-
The EXAFSPAK program suite was developed by one of the authors (G.N.G.) and is available by application in writing to the authors.
-
-
-
-
21
-
-
0024322271
-
-
George, G. N.; Kipke, C. A.; Prince, R. C.; Sunde, R. A.; Enemark, J. H.; Cramer, S. P. Biochemistry 1989. 28, 5075-5080.
-
(1989)
Biochemistry
, vol.28
, pp. 5075-5080
-
-
George, G.N.1
Kipke, C.A.2
Prince, R.C.3
Sunde, R.A.4
Enemark, J.H.5
Cramer, S.P.6
-
24
-
-
49649145902
-
-
Double integration of EPR spectra was performed using a 1 mM CuEDTA standard with correction for transition probability [Aasa, R.; Vånngård. T. J. Magn. Reson. 1975, 19, 308-315].
-
(1975)
J. Magn. Reson.
, vol.19
, pp. 308-315
-
-
Aasa, R.1
Vånngård, T.2
-
25
-
-
13344258353
-
-
Sykes, A. G., Ed.; Academic Press: London
-
Cramer, S. P. Advances in Inorganic and Bioinorganic Mechanisms; Sykes, A. G., Ed.; Academic Press: London, 1983; Vol 2, pp 529-316.
-
(1983)
Advances in Inorganic and Bioinorganic Mechanisms
, vol.2
, pp. 529-1316
-
-
Cramer, S.P.1
-
26
-
-
0039667195
-
-
Kutzler, F. W.; Natoli, C. R.; Misemer, D. K.; Doniach, S.; Hodgson. K. O. J. Chem. Phys. 1980, 73, 3274-3288.
-
(1980)
J. Chem. Phys.
, vol.73
, pp. 3274-3288
-
-
Kutzler, F.W.1
Natoli, C.R.2
Misemer, D.K.3
Doniach, S.4
Hodgson, K.O.5
-
28
-
-
0028961901
-
-
Chan, M. K.; Mukund, S.; Kietzin, A.: Adams, M. W. W.; Ress, D. C. Science 1995, 267, 1463-1469.
-
(1995)
Science
, vol.267
, pp. 1463-1469
-
-
Chan, M.K.1
Mukund, S.2
Kietzin, A.3
Adams, M.W.W.4
Ress, D.C.5
-
30
-
-
0028118254
-
-
Das, S. K.; Chaudhury, P. K.; Biswas, D.; Sarkar, S. J. Am. Chem. Soc. 1994, 116, 9061-9070.
-
(1994)
J. Am. Chem. Soc.
, vol.116
, pp. 9061-9070
-
-
Das, S.K.1
Chaudhury, P.K.2
Biswas, D.3
Sarkar, S.4
-
31
-
-
0000720440
-
-
Long 2.9 Å Cu-S(methionine) EXAFS has previously proved impossible to detect in plastocyanin, even when using polarized single crystal EXAFS to provide the most favorable conditions for detection. See: Penner-Hahn, J. E.; Murata, M.: Hodgson, K. Ï.; Freeman. H. Inorg. Chem. 1989, 28, 1826-1832.
-
(1989)
Inorg. Chem.
, vol.28
, pp. 1826-1832
-
-
Penner-Hahn, J.E.1
Murata, M.2
Hodgson, K.Ï.3
Freeman, H.4
-
32
-
-
13344281740
-
-
Boyde, S.; Ellis, S. R.; Garner, C. D.; Clegg, W. J. Am. Chem. Soc. 1986, 108, 1541-1543.
-
(1986)
J. Am. Chem. Soc.
, vol.108
, pp. 1541-1543
-
-
Boyde, S.1
Ellis, S.R.2
Garner, C.D.3
Clegg, W.4
-
33
-
-
13344296562
-
-
note
-
31, and assuming that the non-sulfur ligands are oxygens (rather than nitrogen).
-
-
-
-
37
-
-
0024506359
-
-
George, G. N.; Turner, N. A.; Bray, R. C.; Morpeth, F. F.; Boxer, D. H.; Cramer, S. P. Biochem. J. 1989, 259, 693-700. Note that an earlier study on enzyme prepared using a different purifation method gave quite different EXAFS results [Cramer, S. P.; Solmonson, L. P.; Adams, M. W. W.; Mortenson, L. E. J. Am. Chem. Soc. 1984, 106, 1467-1471]. The earlier study reported long-distance interactions to an unknown scatterer at about 2.7 Å, and it seems likely that the active site can adopt at least two different structures.
-
(1989)
Biochem. J.
, vol.259
, pp. 693-700
-
-
George, G.N.1
Turner, N.A.2
Bray, R.C.3
Morpeth, F.F.4
Boxer, D.H.5
Cramer, S.P.6
-
38
-
-
0001380448
-
-
George, G. N.; Turner, N. A.; Bray, R. C.; Morpeth, F. F.; Boxer, D. H.; Cramer, S. P. Biochem. J. 1989, 259, 693-700. Note that an earlier study on enzyme prepared using a different purifation method gave quite different EXAFS results [Cramer, S. P.; Solmonson, L. P.; Adams, M. W. W.; Mortenson, L. E. J. Am. Chem. Soc. 1984, 106, 1467-1471]. The earlier study reported long-distance interactions to an unknown scatterer at about 2.7 Å, and it seems likely that the active site can adopt at least two different structures.
-
(1984)
J. Am. Chem. Soc.
, vol.106
, pp. 1467-1471
-
-
Cramer, S.P.1
Solmonson, L.P.2
Adams, M.W.W.3
Mortenson, L.E.4
-
39
-
-
0021810531
-
-
George, G. N.; Bray, R. C.; Morpeth, F. F.; Boxer. D. H. Biochem. J. 1985, 227, 925-931.
-
(1985)
Biochem. J.
, vol.227
, pp. 925-931
-
-
George, G.N.1
Bray, R.C.2
Morpeth, F.F.3
Boxer, D.H.4
-
40
-
-
0023268434
-
-
Turner, N.; Belarmino, B.; Bray, R. C.; Deistung, J.; Le Gall, J.; Moura, J. J. G. Biochem. J. 1987, 243, 755-761.
-
(1987)
Biochem. J.
, vol.243
, pp. 755-761
-
-
Turner, N.1
Belarmino, B.2
Bray, R.C.3
Deistung, J.4
Le Gall, J.5
Moura, J.J.G.6
-
41
-
-
0018109126
-
-
Gutteridge, S. P.; Tanner, S. J.; Bray, R. C. Biochem. J. 1978, 175, 887-897.
-
(1978)
Biochem. J.
, vol.175
, pp. 887-897
-
-
Gutteridge, S.P.1
Tanner, S.J.2
Bray, R.C.3
-
43
-
-
0008155552
-
-
Gheller, S. F.; Schultz, B. E.; Scott, M. J.; Holm, R. H. J. Am. Chem. Soc. 1992, 114, 6934-6935.
-
(1992)
J. Am. Chem. Soc.
, vol.114
, pp. 6934-6935
-
-
Gheller, S.F.1
Schultz, B.E.2
Scott, M.J.3
Holm, R.H.4
-
44
-
-
33751553059
-
-
Roberts, S. A.; Young, C. G.; Kipke, C. A.; Cleland, W. E., Jr.: Yamanouchi, K.; Carducci, M. D.: Enemark, J. H. Inorg. Chem. 1988, 29, 3650-3656.
-
(1988)
Inorg. Chem.
, vol.29
, pp. 3650-3656
-
-
Roberts, S.A.1
Young, C.G.2
Kipke, C.A.3
Cleland Jr., W.E.4
Yamanouchi, K.5
Carducci, M.D.6
Enemark, J.H.7
-
47
-
-
0023655717
-
-
While molybdenum cis di-oxo enzymes such as sulfite oxidase may indeed function by oxo transfer, there is some doubt about the molybdenum hydroxylases such as xanthine oxidase which contain molybdenum oxothiolato active sites. For these enzymes such a mechanism would involve breaking of the strong Mo=O bond, and destabilization of this by Mo=S (as opposed to another Mo=O) is likely to be subtle at best. While concrete evidence does exist for catalytic oxygen exchange with a solvent-exchangeable water in xanthine oxidase [see: Hille, R.: Sprecher, H. J. Biol. Chem. 1987, 262, 10914-10917]; however, direct evidence for a Mo=O transfer mechanism in the molybdenum hydroxylases is lacking.
-
(1987)
J. Biol. Chem.
, vol.262
, pp. 10914-10917
-
-
Hille, R.1
Sprecher, H.2
|