Quantitative Structure–Activity Relationships in Two-Electron Reduction of Nitroaromatic Compounds by Enterobacter cloacae NAD(P)H:Nitroreductase

Nivinskas, Henrikas; Koder, Ronald L.; Anusevičius, Žilvinas; Šarlauskas, Jonas; Miller, Anne‐Frances; Č≐nas, Narimantas

doi:10.1006/abbi.2000.2127

Cited by 56 publications

(76 citation statements)

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“…4B), which is less effi-369 cient than in the case of E. cloacae NR (K i = 0.06 lM [7]), or 370 mammalian NAD(P)H: quinone oxidoreductase (NQO1, K i = 0.01 -371 lM [40]). …”

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confidence: 94%

“…3A). This reaction was accompanied place during E. cloacae NR-catalyzed reaction [7], with a final for-262 mation of product(s) absorbing at 380-385 nm (Fig. 3B) ous media is irreversible [35].…”

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confidence: 95%

“…4A) [17], and E. cloacae NR, >1000 s À1 [7]. The comparison of presteady-380 and steady-state kinetic data of Prx-NR (Fig.…”

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confidence: 97%

“…Enterobacter cloacae nitroreductase [2,[7][8][9], Vibrio fisheri FMN-54 reductase [10], and Thermus thermophilus NADH-oxidase [11]. 55 The physiological role(s) of NRs are unclear except their possible 56 antioxidant functions, because they are induced by oxidative stress 57 and other environmental hazards [12].…”

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confidence: 99%

“…Except for the more de-70 tailed examination of E. cloacae NR [7,16], most kinetic studies of 71 other NRs were confined to a limited number of oxidants with some-72 times poorly characterized reduction thermodynamics ( [3,6,17] were synthesized as described previously [7]. tion mixture as described [7]. The solutions of NaNO 2 (10-100 lM)…”

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confidence: 99%

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Quinone- and nitroreductase reactions of Thermotoga maritima peroxiredoxin–nitroreductase hybrid enzyme

Anusevičius

Misevičienė

Šarlauskas

et al. 2012

Archives of Biochemistry and Biophysics

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a b s t r a c t 25Thermotoga maritima peroxiredoxin-nitroreductase hybrid enzyme (Prx-NR) consists of a ing nitroreductase (NR) domain fused to a peroxiredoxin (Prx) domain. These domains seem to function 27 independently as no electron transfer occurs between them. The reduction of quinones and nitroaromat-28 ics by NR proceeded in a two-electron manner, and follows a 'ping-pong' scheme with sometimes pro-29 nounced inhibition by quinone substrate. The comparison of steady-and presteady-state kinetic data 30 shows that in most cases, the oxidative half-reaction may be rate-limiting in the catalytic cycle of NR. 31The enzyme was inhibited by dicumarol, a classical inhibitor of oxygen-insensitive nitroreductases.

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“…4B), which is less effi-369 cient than in the case of E. cloacae NR (K i = 0.06 lM [7]), or 370 mammalian NAD(P)H: quinone oxidoreductase (NQO1, K i = 0.01 -371 lM [40]). …”

mentioning

confidence: 94%

mentioning

confidence: 95%

“…4A) [17], and E. cloacae NR, >1000 s À1 [7]. The comparison of presteady-380 and steady-state kinetic data of Prx-NR (Fig.…”

mentioning

confidence: 97%

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confidence: 99%

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confidence: 99%

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Quinone- and nitroreductase reactions of Thermotoga maritima peroxiredoxin–nitroreductase hybrid enzyme

Anusevičius

Misevičienė

Šarlauskas

et al. 2012

Archives of Biochemistry and Biophysics

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Meisenheimer Complexes

2010

Comprehensive Organic Name Reactions and Reagents

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This complex has been first reported from the reaction between picryl ether and potassium alkoxide and later it has been isolated and characterized. The stable or transient anionic σ complexes formed from electron‐deficient aromatic compounds and a variety of organic and inorganic bases are generally referred to as the Meisenheimer complexes. It has been reported that these complexes are formed as the intermediates of most nucleophilic aromatic substitution (S N Ar) reactions with two‐step mechanisms. Many nucleophiles have been categorized for the formation of this complex. Kinetically, the nucleophile would preferentially add to the meta ‐position of the leaving group but some of the places K3T1 regioselectivity has been observed. The formation of the Meisenheimer complexes has been modified using a micellar catalyst or by electrochemical reduction. This complex has been involved in various nucleophilic aromatic substitution reactions.

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Conversion of a Dehalogenase into a Nitroreductase by Swapping its Flavin Cofactor with a 5‐Deazaflavin Analogue

Boucher

Rokita

2017

Angewandte Chemie

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Natural and engineered nitroreductases have rarely supported full reduction of nitroaromatics to their amine products,a nd more typically,t ransformations are limited to formation of the hydroxylamine intermediates.Efficient use of these enzymes also requires ar egenerating system for NAD-(P)H to avoid the costs associated with this natural reductant. Iodotyrosine deiodinase is am ember of the same structural superfamily as many nitroreductases but does not directly consume reducing equivalents from NAD(P)H, nor demonstrate nitroreductase activity.H owever,e xchange of its flavin cofactor with a5 -deazaflavin analogue dramatically suppresses its native deiodinase activity and leads to significant nitroreductase activity that supports full reduction to an amine product in the presence of the convenient and inexpensive NaBH 4 .

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Quantitative Structure–Activity Relationships in Two-Electron Reduction of Nitroaromatic Compounds by Enterobacter cloacae NAD(P)H:Nitroreductase

Cited by 56 publications

References 36 publications

Quinone- and nitroreductase reactions of Thermotoga maritima peroxiredoxin–nitroreductase hybrid enzyme

Quinone- and nitroreductase reactions of Thermotoga maritima peroxiredoxin–nitroreductase hybrid enzyme

Meisenheimer Complexes

Conversion of a Dehalogenase into a Nitroreductase by Swapping its Flavin Cofactor with a 5‐Deazaflavin Analogue

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