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1 d varying from 2.0 for glucose to 1.29 for 4-nitrocatechol.
2 3-methyl-5-nitrocatechol (3M5NC), 3-methyl-4-nitrocatechol (3M4NC), and a negligible amount of 3-meth
3 ations predicted the formation of 3-methyl-5-nitrocatechol (3M5NC), 3-methyl-4-nitrocatechol (3M4NC),
5 dihydroxybenzoic acid (PCA), the inhibitor 4-nitrocatechol (4-NC), or cyanide (CN(-)) have been solve
6 s whereas 3-methyl-4-nitrophenol, 3-methyl-4-nitrocatechol, 4-nitrophenol, 3-nitrophenol, and 4-chlor
7 ectable by using the alternative substrate 4-nitrocatechol (4NC) and mutation of the active site His2
8 ng cleavage of the electron-poor substrate 4-nitrocatechol (4NC) by Co(II)-homoprotocatechuate 2,3-di
9 ing reaction of the chromophoric substrate 4-nitrocatechol (4NC) is shown to proceed with rate consta
10 red by utilizing the alternative substrate 4-nitrocatechol (4NC), which is also cleaved in the proxim
12 ative, iron(II) soybean lipoxygenase 3 and 4-nitrocatechol, a known inhibitor of the enzyme, has been
13 pe NDO, and that produced 3-amino-4-methyl-5-nitrocatechol and 2-amino-4,6-dinitrobenzyl alcohol from
15 edict more than one stable complex between 4-nitrocatechol and the central cavity of lipoxygenase 3,
17 strates, including homoprotocatechuate and p-nitrocatechol, are nonessential activators of the catala
18 III)-O2(-) pair found for the O2 adduct of 4-nitrocatechol-bound homoprotocatechuate 2,3-dioxygenase.
19 mandelate, or the tight-binding inhibitor, p-nitrocatechol, but not in the complexes with weaker bind
20 rophenol C6H5NO3, methylnitrophenol C7H7NO3, nitrocatechol C6H5NO4, methylnitrocatechol C7H7NO4, and
23 ive, simple assay for the determination of 4-nitrocatechol formed during the P450-dependent hydroxyla
24 eated variant F350T that produced 3-methyl-4-nitrocatechol from 2,6-dinitrotoluene (26DNT), that rele
26 on makes it possible to detect 0.5 pmol of 4-nitrocatechol injected, 30 times less than previously re
31 eractions with COMT were established via the nitrocatechol ring, allowing derivatization of the side
32 substrate mimicking competitive inhibitor p-nitrocatechol sulfate (PNC) is used as a probe of the ac
33 Using a specific colorimetric substrate para-nitrocatechol sulfate (pNCS), detectable ASA residual ac
34 a specific YopH small molecule inhibitor, p-nitrocatechol sulfate (pNCS), which exhibits a Ki value
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