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1 s of the protein-derived cofactor tryptophan tryptophylquinone.
3 ologic electron transfer from the tryptophan tryptophylquinone cofactor of MADH to heme via the coppe
4 ay for electron-transfer from the tryptophan tryptophylquinone cofactor of MADH to the copper of amic
5 talyze formation of a Trp-derived tryptophan tryptophylquinone cofactor on its substrate protein, pre
6 residues to generate a catalytic tryptophan tryptophylquinone cofactor within methylamine dehydrogen
10 e structure determination of this tryptophan tryptophylquinone-containing enzyme from Methylobacteriu
11 a glycine oxidase that possesses a cysteine tryptophylquinone (CTQ) cofactor that is formed by postt
12 e dehydrogenase (QHNDH) possesses a cysteine tryptophylquinone (CTQ) prosthetic group that catalyzes
13 ontained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-m
14 ylamine dehydrogenase (MADH) is a tryptophan tryptophylquinone-dependent enzyme that catalyzes the ox
17 lectron oxidation that results in tryptophan tryptophylquinone formation occurs in three discrete two
18 king of collagen and elastin; (c) tryptophan tryptophylquinone of alkylamine dehydrogenases from gram
21 , this cofactor may be identical to cysteine tryptophylquinone, recently described in the bacterial q
22 required for the biosynthesis of tryptophan tryptophylquinone, the prosthetic group of methylamine d
23 contains incompletely synthesized tryptophan tryptophylquinone, to the bis-Fe(IV) form of MauG is bes
24 se (MADH) utilizes its endogenous tryptophan tryptophylquinone (TTQ) as a cofactor in enzymatic catal
25 lectrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of AADH to the type I c
26 lectrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of MADH to the type 1 c
27 o tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrog
32 l other enzymes containing CTQ or tryptophan tryptophylquinone (TTQ) cofactors are dehydrogenases.
33 ylamine dehydrogenase (MADH) is a tryptophan tryptophylquinone (TTQ) dependent enzyme that catalyzes
34 yme containing a quinone cofactor tryptophan tryptophylquinone (TTQ) derived from two tryptophan resi
35 iogenesis of the quinone cofactor tryptophan tryptophylquinone (TTQ) in methylamine dehydrogenase (MA
36 The two-electron oxidation of tryptophan tryptophylquinone (TTQ) in substrate-reduced methylamine
38 obtained from redox studies of a tryptophan tryptophylquinone (TTQ) model compound for which the two
39 tron transfer (ET) occurs between tryptophan tryptophylquinone (TTQ) of MADH and the type I copper of
40 eaction from the reduced O-quinol tryptophan tryptophylquinone (TTQ) of MADH to oxidized amicyanin ar
41 transfer (ET) occurs between the tryptophan tryptophylquinone (TTQ) prosthetic group of aromatic ami
43 o the periplasm, synthesis of the tryptophan tryptophylquinone (TTQ) prosthetic group, and formation
45 x, electrons are transferred from tryptophan tryptophylquinone (TTQ) to heme via the type I copper ce
46 eMADH) with partially synthesized tryptophan tryptophylquinone (TTQ) to yield the mature protein with
47 ains the protein-derived cofactor tryptophan tryptophylquinone (TTQ) which is generated by the posttr
49 auG catalyzes the biosynthesis of tryptophan tryptophylquinone (TTQ), the protein-derived cofactor of
52 he active cofactor is presumably a histidine tryptophylquinone, which has not been previously describ
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