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1 tryptophan tryptophylquinone cofactor within methylamine dehydrogenase.
2 n tryptophylquinone, the prosthetic group of methylamine dehydrogenase.
5 rent from those for the related quinoprotein methylamine dehydrogenase and its associated redox prote
6 es, methylotrophy is enabled by methanol and methylamine dehydrogenases and their specific electron t
7 ee-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans
8 ese data in which the reduction of Cu(2+) by methylamine dehydrogenase is a true ET reaction while th
9 tophylquinone (TTQ), the prosthetic group of methylamine dehydrogenase, is formed by post-translation
12 tentials for the oxidized/reduced couples of methylamine dehydrogenase (MADH) and aromatic amine dehy
13 pared with the complex of the TTQ-containing methylamine dehydrogenase (MADH) and the cupredoxin amic
14 s for methylamine oxidation: the periplasmic methylamine dehydrogenase (MaDH) and the cytoplasmic N-m
15 tryptophylquinone (TTQ) in substrate-reduced methylamine dehydrogenase (MADH) by amicyanin is known t
21 factor tryptophan tryptophylquinone (TTQ) in methylamine dehydrogenase (MADH) involves the post-trans
25 yptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase (MADH) is covalently modified
26 yptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase (MADH) is covalently modified
30 in that mediates electron transfer (ET) from methylamine dehydrogenase (MADH) to cytochrome c-551i.
32 he diheme enzyme MauG and different forms of methylamine dehydrogenase (MADH) were subjected to kinet
36 Contrary to the TTQ-containing subunit of methylamine dehydrogenase (MADH), which is catalytically
43 talyzes posttranslational modifications of a methylamine dehydrogenase precursor protein to generate
44 nal modification of the precursor protein of methylamine dehydrogenase (preMADH) to complete biosynth
45 ional modification of a precursor protein of methylamine dehydrogenase (preMADH) to complete the bios
46 ation of a biosynthetic precursor protein of methylamine dehydrogenase (PreMADH) with partially synth
47 -studied aerobic methylotroph, a periplasmic methylamine dehydrogenase that catalyzes the primary oxi
49 ectron transfer (ET) reactions from O-quinol methylamine dehydrogenase to oxidized native and mutant
51 related to M. extorquens AM1 but is lacking methylamine dehydrogenase, to dissect the genetics and p
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