Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transfer
Keyword(s):
The extent of charge delocalization throughout the diheme redox center of MauG influences the reorganization energy associated with the electron transfer reactions to the high-valent hemes. This explains how enzymes can optimize various reactions by utilizing different high-valent redox centers.
1991 ◽
Vol 180
(4)
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pp. 353-357
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2003 ◽
Vol 107
(48)
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pp. 13255-13257
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2003 ◽
Vol 125
(48)
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pp. 14714-14715
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1998 ◽
Vol 285
(3-4)
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pp. 150-154
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2001 ◽
Vol 73
(3)
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pp. 519-523
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1995 ◽
Vol 117
(4)
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pp. 1411-1421
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1996 ◽
Vol 100
(35)
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pp. 14688-14693
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