Structural Studies of Two Mutants of Amicyanin from Paracoccus denitrificans That Stabilize the Reduced State of the Copper

Mutation of Pro94 to phenylalanine or alanine significantly alters the redox properties of the type I copper center of amicyanin. Each mutation increases the redox midpoint potential (E m) value by at least 140 mV and shifts the pK a for the pH dependence of the E m value to a more acidic value. Ato...

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Veröffentlicht in:	Biochemistry (Easton) 2004-07, Vol.43 (29), p.9372-9380
Hauptverfasser:	Carrell, Christopher J, Sun, Dapeng, Jiang, Shoulei, Davidson, Victor L, Mathews, F. Scott
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Bacterial Proteins - genetics Copper - chemistry Hydrogen Bonding Models, Molecular Mutation Paracoccus denitrificans Paracoccus denitrificans - chemistry
Online-Zugang:	Volltext
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