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1 biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.
3 r the physiologic electron transfer from the tryptophan tryptophylquinone cofactor of MADH to heme vi
4 icted pathway for electron-transfer from the tryptophan tryptophylquinone cofactor of MADH to the cop
5 istry to catalyze formation of a Trp-derived tryptophan tryptophylquinone cofactor on its substrate p
6 tryptophan residues to generate a catalytic tryptophan tryptophylquinone cofactor within methylamine
8 e report the structure determination of this tryptophan tryptophylquinone-containing enzyme from Meth
10 usual six-electron oxidation that results in tryptophan tryptophylquinone formation occurs in three d
11 r cross-linking of collagen and elastin; (c) tryptophan tryptophylquinone of alkylamine dehydrogenase
14 in which is required for the biosynthesis of tryptophan tryptophylquinone, the prosthetic group of me
15 ADH, which contains incompletely synthesized tryptophan tryptophylquinone, to the bis-Fe(IV) form of
16 dehydrogenase (MADH) utilizes its endogenous tryptophan tryptophylquinone (TTQ) as a cofactor in enzy
18 hin which electrons are transferred from the tryptophan tryptophylquinone (TTQ) cofactor of MADH to t
21 ation of two tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor of methylami
26 ) is an enzyme containing a quinone cofactor tryptophan tryptophylquinone (TTQ) derived from two tryp
30 om what was obtained from redox studies of a tryptophan tryptophylquinone (TTQ) model compound for wh
31 ecular electron transfer (ET) occurs between tryptophan tryptophylquinone (TTQ) of MADH and the type
32 e true ET reaction from the reduced O-quinol tryptophan tryptophylquinone (TTQ) of MADH to oxidized a
33 in electron transfer (ET) occurs between the tryptophan tryptophylquinone (TTQ) prosthetic group of a
34 ses and is required for the synthesis of the tryptophan tryptophylquinone (TTQ) prosthetic group of M
35 e protein to the periplasm, synthesis of the tryptophan tryptophylquinone (TTQ) prosthetic group, and
37 551i complex, electrons are transferred from tryptophan tryptophylquinone (TTQ) to heme via the type
38 ogenase (PreMADH) with partially synthesized tryptophan tryptophylquinone (TTQ) to yield the mature p
39 (MADH) contains the protein-derived cofactor tryptophan tryptophylquinone (TTQ) which is generated by
41 me enzyme MauG catalyzes the biosynthesis of tryptophan tryptophylquinone (TTQ), the protein-derived
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