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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),
4 M4NC), and a negligible amount of 3-methyl-6-nitrocatechol (3M6NC).
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
11 huate (HPCA) and the alternative substrate 4-nitrocatechol (4NC).
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
14                  Purified ARSK turned over p-nitrocatechol and p-nitrophenyl sulfate.
15 edict more than one stable complex between 4-nitrocatechol and the central cavity of lipoxygenase 3,
16                                    MNC and 4-nitrocatechol are good substrates whereas 3-methyl-4-nit
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
21                                          New nitrocatechol COMT inhibitors based on naturally occurri
22                                          All nitrocatechol derivatives displayed potent inhibition of
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
25 oxygenase was soaked in the slow substrate 4-nitrocatechol in a low O2 atmosphere.
26 on makes it possible to detect 0.5 pmol of 4-nitrocatechol injected, 30 times less than previously re
27                                            p-Nitrocatechol is shown to bind differently to 2,3-HPCD t
28  initial oxidation of DNT to form 4-methyl-5-nitrocatechol (MNC) and nitrite.
29                                   4-Methyl-5-nitrocatechol (MNC) is an intermediate in the degradatio
30                                   However, 4-nitrocatechol oxidation was completely quenched in the p
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
35                       Using the docking of p-nitrocatechol sulfate to Yersinia protein tyrosine phosp
36          In addition, the sulfate group of p-nitrocatechol sulfate was found to be important both in
37             Oxidation of 4-nitrophenol and 4-nitrocatechol was observed for both derivatives.

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