Structure, Protonation State and Dynamics of Catalase Compound II

Rovira, Carme

doi:10.1002/cphc.200400633

Cited by 42 publications

(57 citation statements)

References 29 publications

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“…The relatively long (1.81 Å) iron-oxygen bond in CYP119-II indicates that this compound II derivative likely contains an ironhydroxide moiety. It is in the range of bond lengths predicted computationally for a porphyrin-iron(IV) hydroxide species (48,49), and long iron-oxygen bonds have long been thought to be the signature of protonated ferryl-oxo species in compound II species (36,39,47). Accordingly, one concludes that the ferryloxo species in CYP119-II is basic such that the oxygen atom is protonated at neutral pH.…”

Section: Resultsmentioning

confidence: 95%

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Newcomb

Halgrimson

Horner

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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The cytochrome P450 enzyme CYP119, its compound II derivative, and its nitrosyl complex were studied by iron K-edge x-ray absorption spectroscopy. The compound II derivative was prepared by reaction of the resting enzyme with peroxynitrite and had a lifetime of Ϸ10 s at 23°C. The CYP119 nitrosyl complex was prepared by reaction of the enzyme with nitrogen monoxide gas or with a nitrosyl donor and was stable at 23°C for hours. Samples of CYP119 and its derivatives were studied by x-ray absorption spectroscopy at temperatures below 140 (K) at the Advanced Photon Source of Argonne National Laboratory. The x-ray absorption near-edge structure spectra displayed shifts in edge and pre-edge energies consistent with increasing effective positive charge on iron in the series native CYP119 < CYP119 nitrosyl complex < CYP119 compound II derivative. Extended x-ray absorption fine structure spectra were simulated with good fits for k ‫؍‬ 12 Å ؊1 for native CYP119 and k ‫؍‬ 13 Å ؊1 for both the nitrosyl complex and the compound II derivative. The important structural features for the compound II derivative were an iron-oxygen bond length of 1.82 Å and an iron-sulfur bond length of 2.24 Å, both of which indicate an iron-oxygen single bond in a ferryl-hydroxide, Fe IV OH, moiety.EXAFS ͉ ferryl-oxo ͉ XANES

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Section: Resultsmentioning

confidence: 95%

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Newcomb

Halgrimson

Horner

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…The cyanoguanidine group of cimetidine may interact with the negative charge of Glu51. The structural change imposed by this interaction can affect the position of His55 and make it far from Asn128, the cooperation of which is essential for the enzyme activity [Chelikani et al, 2003;Rovira, 2005]. The present experiments showed that, in contrast to cimetidine, another H 2 receptor blocker drug, ranitidine, had no effect on the activity of catalase.…”

Section: Discussionmentioning

confidence: 42%

Effect of Cimetidine on Catalase Activity of <b><i>Pseudomonas aeruginosa: </i></b> A Suggested Mechanism of Action

Masoud

Ebrahimi²,

Minai-Tehrani³

2014

Microb Physiol

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Catalase is an important enzyme for the degradation of hydrogen peroxide in cells. Bacteria have potent catalase to deal with H₂O₂ in their medium culture. Any chemicals that inhibit catalase activity can be harmful for cells. Histamine H₂ antagonist drugs such as cimetidine and ranitidine are used for the treatment of gastrointestinal tract disorders. The present results showed that cimetidine could inhibit the catalase activity of Pseudomonas aeruginosa in a competitive inhibition. The determination of IC₅₀ value and K_i (6.5 μM) of cimetidine demonstrated that the enzyme binds to the drug with high affinity. Binding of the drug to the enzyme was pH-dependent and no binding was observed at basic pH (>9) and acidic pH (<6). Moreover, the imidazole ring and cyanoguanidine group of cimetidine may play an important role in inhibition by binding to Fe in heme group and glutamic acid 51 residue on the enzyme, respectively. Ranitidine had no effect on the catalase activity.

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“…Formation of compound II and III has been described elsewhere (Kirkman et al, 1999;Rovira, 2005). The haem group in catalase is vital to the reaction, because Fe(III) bound at the center of porphyrin ring can be oxidised to the very oxidised and less common Fe(IV), or ferryl species.…”

Section: Mechanism Of Actionmentioning

confidence: 99%

Human catalase: looking for complete identity

2010

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Catalases are well studied enzymes that play critical roles in protecting cells against the toxic effects of hydrogen peroxide. The ubiquity of the enzyme and the availability of substrates made heme catalases the focus of many biochemical and molecular biology studies over 100 years. In human, this has been implicated in various physiological and pathological conditions. Advancement in proteomics revealed many of novel and previously unknown features of this mysterious enzyme, but some functional aspects are yet to be explained. Along with discussion on future research area, this mini-review compile the information available on the structure, function and mechanism of action of human catalase.

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Structure, Protonation State and Dynamics of Catalase Compound II

Cited by 42 publications

References 29 publications

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

X-ray absorption spectroscopic characterization of a cytochrome P450 compound II derivative

Effect of Cimetidine on Catalase Activity of <b><i>Pseudomonas aeruginosa: </i></b> A Suggested Mechanism of Action

Human catalase: looking for complete identity

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