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1 s of the protein-derived cofactor tryptophan tryptophylquinone.
2               The biosynthesis of tryptophan tryptophylquinone, a protein-derived cofactor, involves
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
7 ne dehydrogenase, which possesses a cysteine tryptophylquinone cofactor.
8 s active and appears to possess a functional tryptophylquinone cofactor.
9 e precursor protein to generate a tryptophan tryptophylquinone cofactor.
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 cea (PlGoxA) uses a protein-derived cysteine tryptophylquinone (CTQ) cofactor to catalyze conversion
13 ase that utilizes a protein-derived cysteine tryptophylquinone (CTQ) cofactor.
14 e dehydrogenase (QHNDH) possesses a cysteine tryptophylquinone (CTQ) prosthetic group that catalyzes
15 ontained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-m
16 ylamine dehydrogenase (MADH) is a tryptophan tryptophylquinone-dependent enzyme that catalyzes the ox
17                       It is the second known tryptophylquinone enzyme to function as an oxidase, the
18 ructurally conserved in this position in all tryptophylquinone enzymes.
19  of structurally conserved residues of other tryptophylquinone enzymes.
20 lectron oxidation that results in tryptophan tryptophylquinone formation occurs in three discrete two
21 king of collagen and elastin; (c) tryptophan tryptophylquinone of alkylamine dehydrogenases from gram
22      ET from the reduced O-quinol tryptophan tryptophylquinone of MADH to oxidized P94A amicyanin is
23 bilized enzyme that possesses the tryptophan tryptophylquinone prosthetic group.
24 , this cofactor may be identical to cysteine tryptophylquinone, recently described in the bacterial q
25  required for the biosynthesis of tryptophan tryptophylquinone, the prosthetic group of methylamine d
26 contains incompletely synthesized tryptophan tryptophylquinone, to the bis-Fe(IV) form of MauG is bes
27 se (MADH) utilizes its endogenous tryptophan tryptophylquinone (TTQ) as a cofactor in enzymatic catal
28 lectrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of AADH to the type I c
29 lectrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of MADH to the type 1 c
30 o tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrog
31                               The tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrog
32                               The tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrog
33 osynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor.
34 osynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor.
35 l other enzymes containing CTQ or tryptophan tryptophylquinone (TTQ) cofactors are dehydrogenases.
36 ylamine dehydrogenase (MADH) is a tryptophan tryptophylquinone (TTQ) dependent enzyme that catalyzes
37 yme containing a quinone cofactor tryptophan tryptophylquinone (TTQ) derived from two tryptophan resi
38 iogenesis of the quinone cofactor tryptophan tryptophylquinone (TTQ) in methylamine dehydrogenase (MA
39     The two-electron oxidation of tryptophan tryptophylquinone (TTQ) in substrate-reduced methylamine
40                                   Tryptophan tryptophylquinone (TTQ) is the protein-derived cofactor
41  obtained from redox studies of a tryptophan tryptophylquinone (TTQ) model compound for which the two
42 tron transfer (ET) occurs between tryptophan tryptophylquinone (TTQ) of MADH and the type I copper of
43 eaction from the reduced O-quinol tryptophan tryptophylquinone (TTQ) of MADH to oxidized amicyanin ar
44  transfer (ET) occurs between the tryptophan tryptophylquinone (TTQ) prosthetic group of aromatic ami
45 required for the synthesis of the tryptophan tryptophylquinone (TTQ) prosthetic group of MADH.
46 o the periplasm, synthesis of the tryptophan tryptophylquinone (TTQ) prosthetic group, and formation
47 smaller beta subunit possessing a tryptophan tryptophylquinone (TTQ) prosthetic group.
48 x, electrons are transferred from tryptophan tryptophylquinone (TTQ) to heme via the type I copper ce
49 eMADH) with partially synthesized tryptophan tryptophylquinone (TTQ) to yield the mature protein with
50 ains the protein-derived cofactor tryptophan tryptophylquinone (TTQ) which is generated by the posttr
51                                   Tryptophan tryptophylquinone (TTQ), the prosthetic group of methyla
52 auG catalyzes the biosynthesis of tryptophan tryptophylquinone (TTQ), the protein-derived cofactor of
53 form the protein-derived cofactor tryptophan tryptophylquinone (TTQ).
54 hat form the unique redox center, tryptophan tryptophylquinone (TTQ).
55 he active cofactor is presumably a histidine tryptophylquinone, which has not been previously describ