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Title
Organism
1.4.9.1
Copper-binding energetics of amicyanin in different folding states
Paracoccus denitrificans
1.4.9.1
Free-energy landscape and proton transfer pathways in oxidative deamination by methylamine dehydrogenase
Paracoccus denitrificans
1.4.9.1
Identification of genes essential for the biogenesis of quinohemoprotein amine dehydrogenase
Paracoccus denitrificans
1.4.9.1
Intra-electron transfer of amicyanin from newly derived active site to redox potential tuned type 1 copper site
Paracoccus denitrificans
1.4.9.1
MauG A di-heme enzyme required for methylamine dehydrogenase maturation
Paracoccus denitrificans
1.4.9.1
MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis
Paracoccus denitrificans
1.4.9.1
Mutation of Trp93 of MauG to tyrosine causes loss of bound Ca2+ and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis
Paracoccus denitrificans
1.4.9.1
Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 A away
Paracoccus denitrificans
1.4.9.1
Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG
Paracoccus denitrificans
1.4.9.1
A single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyanin
Paracoccus denitrificans
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