Hydroxylation of aniline mediated by heme-bound oxy-radicals in a heme peptide model system

Rusvai, E.; Végh, Marcell Zoltán; Kramer, Mihály; Horváth, István

doi:10.1016/0006-2952(88)90675-2

Cited by 30 publications

(15 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In conclusion, our results describe that besides the oxidation of typical peroxidase cosubstrates [2±4], the para-hydroxylation of aniline [5], the monooxygenation of polycyclic aromatic compounds [6], the S-oxidation of sulfides [7], and N-and O-dealkylation reactions [8], MP8 is able to catalyze another type of reaction: the nitration of aromatic compounds like phenol by nitrite in the presence of H 2 O 2 at room temperature and neutral pH. This new activity of MP8 first opens a new access to nitro-aromatic compounds under mild conditions and, because the nitration of l-tyrosine into 3-nitro-l-tyrosine is also observed, it further validates the use of this minienzyme as a model for heme peroxidases, especially to mimick the reactions of NO-derived species such as nitrite and NO 2 X with lipids [16], proteins [17±19], nucleic acids [20], mediators [21] and drugs [22] under oxidative stress conditions.…”

Section: (C)mentioning

confidence: 79%

Microperoxidase 8 catalyzed nitration of phenol by nitrogen dioxide radicals

Ricoux

Boucher

Mansuy

et al. 2001

European Journal of Biochemistry

View full text Add to dashboard Cite

Microperoxidase 8 (MP8) is a heme octapeptide obtained by hydrolytic digestion of horse heart cytochrome c. At pH below 9, the heme iron is axially coordinated to the imidazole side chain of His18 and to a water molecule. Replacement of this weak ligand by H 2 O 2 allows the formation of high-valent iron-oxo species which are responsible for both peroxidase-like and cytochrome P450-like activities of MP8.This paper shows that MP8 is able to catalyze the nitration of phenol by nitrite. The reaction requires H 2 O 2 and is inhibited by ligands having a high affinity for the iron, catalase and radical scavengers. This suggests that the nitrating species could be NO 2 X radicals formed by the oxidation of nitrite by high-valent iron-oxo species.This new activity of MP8 opens a new access to nitroaromatic compounds under mild conditions and validates the use of this minienzyme to mimick heme peroxidases, especially in the reactions of NO-derived species with biomolecules under oxidative stress conditions.

show abstract

Section: (C)mentioning

confidence: 79%

Microperoxidase 8 catalyzed nitration of phenol by nitrogen dioxide radicals

Ricoux

Boucher

Mansuy

et al. 2001

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…In the literature, there are many publications describing the peroxide-dependent P450 analogous and peroxidatic activities of microperoxidases in homogeneous solution [66,[80][81][82][83][84][85][86][87][88][89]. The peroxidatic efficiency of microperoxidases for the oxidation of typical phenolic substrates as expressed by k cat /K M is almost 100 times lower than the value for HRP [90].…”

Section: Microperoxidasesmentioning

confidence: 99%

Can peroxygenase and microperoxidase substitute cytochrome P450 in biosensors

Yarman

Peng

et al. 2011

Bioanal Rev

View full text Add to dashboard Cite

Aromatic peroxygenase (APO) from the basidiomycetous mushroom Agrocybe aegerita (AaeAPO) and microperoxidases (MPs) obtained from cytochrome c exhibit a broad substrate spectrum including hydroxylation of selected aromatic substrates, demethylation and epoxidation by means of hydrogen peroxide. It overlaps with that of cytochrome P450 (P450), making MPs and APOs to alternate recognition elements in biosensors for the detection of typical P450 substrates. Here, we discuss recently developed approaches using microperoxidases and peroxygenases in view of their potential to supplement P450 enzymes as recognition elements in biosensors for aromatic compounds. Starting as early as the 1970s, the direct electron transfer between electrodes and the heme group of heme peptides called microperoxidases has been used as a model of oxidoreductases. These MP-modified electrodes are used as hydrogen peroxide detectors based on the catalytic current generated by electrically contacted microperoxidase molecules. A similar catalytic reaction has been obtained for the electrode-immobilised heme protein AaeAPO. However, up to now, no MP-based sensors for substrates have been described. In this review, we present biosensors which indicate 4-nitrophenol, aniline, naphthalene and p-aminophenol based on the peroxide-dependent substrate conversion by electrode-immobilised MP and AaeAPO. In these enzyme electrodes, the signal is generated by the conversion of all substrates, thus representing in complex media an overall parameter. The performance of these sensors and their further development are discussed in comparison with P450-based electrodes

show abstract

“…First of all, MP8 is able to perform the oxidation of several typical peroxidase co-substrates like o-dianisine [86], ABTS [87], guaiacol [88]. Second, MP8 also catalyzes the para-hydroxylation of aniline [89], the S-oxidation of sulfides [90], the monooxygenation of polycyclic aromatic compounds [91], and the N-and O-dealkylation of aromatic amines and ethers [92]. In addition, MP8 has also been recently shown to be able to oxidize N-monosubstituted hydroxylamines with formation of very stable iron(II)e nitrosoalkane complexes [93] and to catalyze the nitration of phenols by nitrite in the presence of H 2 O 2 [94].…”

Section: Microperoxidase 8 Antibody Complexesmentioning

confidence: 99%