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13044262599
-
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note
-
By perturbed we mean an increase in absorption at 450 nm and a rhombic EPR spectrum.
-
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25
-
-
13044313625
-
-
note
-
This enzyme has a high degree of homology with Polyporus versicolor laccase. It should be noted that Polyporus pinsitis is also referred to as Trametes villosa, and Polyporus versicolor is often referred to as Trametes versicolor.
-
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0000085727
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34
-
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13044293424
-
-
note
-
The imidazole ring orientation used in the calculations was similar to that in the plastocyanin crystal structure; small deviations in ring orientation from the crystal structure of plastocyanin are due to placing the Cu in the trigonal plane.
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35
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33845377800
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-
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13044275684
-
-
note
-
Although the splittings are clearly observed in the spectrum, superhyperfine coupling constants were obtained from EPR simulations.
-
-
-
-
50
-
-
13044280280
-
-
note
-
-1 is obscured by contributions from a small heme impurity.
-
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51
-
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0003658867
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Piepho, S. B., Schatz, P. N., Eds.; John Wiley and Sons: New York
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-
-
13044285467
-
-
note
-
2+ at low temperature arises from C-terms. C-term intensity requires polarization in two perpendicular directions. However, the low symmetry of the blue copper site removes all orbital degeneracy; therefore, transitions are polarized in only one direction. For low-symmetry sites, the only mechanism for C-term intensity involves spin - orbit coupling between states that mix their orthogonal polarizations.
-
-
-
-
54
-
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12044249993
-
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59
-
-
13044270437
-
-
note
-
17).
-
-
-
-
61
-
-
13044270436
-
-
note
-
-1 the transition energy of the intermediate excited state minus the transition energy of the excited state, (2) the cross product of the polarization of the ground state → intermediate excited-state transition with the polarization of the ground state → excited-state transition, and (3) the spin-orbit coupling of the intermediate excited state and the excited state.
-
-
-
-
62
-
-
13044292074
-
-
note
-
-1) x the angular momentum matrix element.
-
-
-
-
64
-
-
13044292076
-
-
note
-
35 and calculations indicate that it is negative.
-
-
-
-
65
-
-
0026355316
-
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Van Pouderoyen, G.6
Canters, G.W.7
Loehr, T.M.8
Sanders-Loehr, J.9
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67
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13044316737
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note
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This is in contrast to the 42% Cu character in plastocyanin determined experimentally from Cu L-edge spectroscopy. The difference between the calculated and experimental Cu character most likely relates to the effects of charge partitioning in the intersphere region and sphere overlap in the calculations.
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68
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0000140532
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Larsson, S.; Broo, A.; Sjölin, L. J. Phys. Chem. 1995, 99, 4860-4865.
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(1995)
J. Phys. Chem.
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, pp. 4860-4865
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Larsson, S.1
Broo, A.2
Sjölin, L.3
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69
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13044273635
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note
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1 representation of the plastocyanin active site. These more recent plastocyanin Xα-SW calculations give a value of 35% for the S character in the HOMO of plastocyanin. The quantitative difference (3%) in S character between these two plastocyanin calculations is due to differences in charge partitioning in the intersphere regions and differences in sphere overlap.
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71
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13044292075
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note
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Relative to intermediate structure B, the small shift in the energy of the xy orbital for the final fungal laccase model likely results from the small increase in the N-Cu-N angle, which places the Cu-N bonds slightly closer to the xy orbital, thereby increasing the antibonding interaction.
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73
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0031827994
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Wittung-Stafshede, P.; Hill, M. G.; Gomez, E.; Di Bilio, A. J.; Karlsson, B. G.; Leckner, J.; Winkler, J. R.; Gray, H. B.; Malmström, B. G. J. Biol. Inorg. Chem. 1998, 3, 367-370.
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(1998)
J. Biol. Inorg. Chem.
, vol.3
, pp. 367-370
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Wittung-Stafshede, P.1
Hill, M.G.2
Gomez, E.3
Di Bilio, A.J.4
Karlsson, B.G.5
Leckner, J.6
Winkler, J.R.7
Gray, H.B.8
Malmström, B.G.9
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74
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0001531848
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Stephens, P. J.; Jollie, D. R.; Warshel, A. Chem. Rev. 1996, 96, 2491-2513.
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(1996)
Chem. Rev.
, vol.96
, pp. 2491-2513
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Stephens, P.J.1
Jollie, D.R.2
Warshel, A.3
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75
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0027536105
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Pascher, T.; Karlsson, B. G.; Nordling, M.; Malmström, B. G.; Vänngård, T. Eur. J. Biochem. 1993, 212, 289-296.
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(1993)
Eur. J. Biochem.
, vol.212
, pp. 289-296
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Pascher, T.1
Karlsson, B.G.2
Nordling, M.3
Malmström, B.G.4
Vänngård, T.5
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76
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0027503415
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Romero, A.; Hoitink, C. W. G.; Nar, H.; Huber, R.; Messerschmidt, A.; Canters, G. W. J. Mol. Biol. 1993, 229, 1007-1021.
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(1993)
J. Mol. Biol.
, vol.229
, pp. 1007-1021
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Romero, A.1
Hoitink, C.W.G.2
Nar, H.3
Huber, R.4
Messerschmidt, A.5
Canters, G.W.6
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77
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13044252903
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Personal communication
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Neese, F. Personal communication.
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Neese, F.1
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78
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13044277017
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note
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As discussed above, this feature is distorted in the fungal laccases because of spectral overlap of the tightly grouped ligand field bands.
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