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Molecular Basis for Interprotein Complex-Dependent Effects on the Redox Properties of Amicyanin
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Electronic Structure of the Reduced Blue Copper Active Site: Contributions to Reduction Potentials and Geometry
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What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Amicyanin and Complexes of Amicyanin with Methylamine Dehydrogenase and Cytochrome c 551 i
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Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy
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inferred← citeshttps://doi.org/10.1016/j.abb.2005.09.016openalex-snapshot
The ligand geometry of copper determines the stability of amicyanin
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The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site
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Characterization of the free energy dependence of an interprotein electron transfer reaction by variation of pH and site-directed mutagenesis
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Substitution of the sole tryptophan of the cupredoxin, amicyanin, with 5-hydroxytryptophan alters fluorescence properties and energy transfer to the type 1 copper site
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inferred← citeshttps://doi.org/10.1016/s0005-2728(00)00052-9openalex-snapshot
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UV resonance Raman and NMR spectroscopic studies on the pH dependent metal ion release from pseudoazurin
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Electron transfer processes of redox proteins at inherently modified microelectrode array devices
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inferred← citeshttps://doi.org/10.1021/bi700303eopenalex-snapshot
Correlation of Rhombic Distortion of the Type 1 Copper Site of M98Q Amicyanin with Increased Electron Transfer Reorganization Energy
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inferred← citeshttps://doi.org/10.1107/s0907444912005343openalex-snapshot
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Mechanisms of Catalysis and Electron Transfer by Tryptophan Tryptophylquinone Enzymes
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