Formation of compound I by the reaction of catalase with peroxoacetic acid.
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ABSTRACT:
SUBMITTER: Jones P
PROVIDER: S-EPMC1174420 | biostudies-other | 1972 Nov
REPOSITORIES: biostudies-other
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Project description:Studies of the pH decreases that accompany the formation of Compound I from ox liver catalase and peroxoacetic acid in unbuffered systems imply that 1 mol of acetic acid is released/mol of catalase ferrihaem Compound I formed. This result is consistent with results previously obtained (Schonbaum & Lo, 1972) for the formation of peroxidase Compound I by using peroxo acid substrate.
| S-EPMC1168406 | biostudies-other
Project description:1. NADPH binds to bovine catalase and to yeast catalases A and T, but not to Escherichia coli catalase HPII. The association was demonstrated using chromatography and fluorimetry. Bound NADPH fluoresces in a similar way to NADPH in solution. 2. Bound NADPH protects bovine and yeast catalases against forming inactive peroxide compound II either via endogenous reductant action or by ferrocyanide reduction during catalytic activity in the presence of slowly generated peroxide. 3. Bound NADPH reduces neither compound I nor compound II of catalase. It apparently reacts with an intermediate formed during the decay of compound I to compound II; this postulated intermediate is an immediate precursor of stable compound II either when the latter is formed by endogenous reductants or when ferrocyanide is used. It represents therefore a new type of hydrogen donor that is not included in the original classification of Keilin and Nicholls [Keilin, D. and Nicholls, P. (1958) Biochim. Biophys. Acta 29, 302-307] 4. A model for NADPH action is presented in which concerted reduction of the ferryl iron and of a neighbouring protein free radical is responsible for the observed NADPH effects. The roles of migrant radical species in mammalian and yeast catalases are compared with similar events in metmyoglobin and cytochrome c peroxidase reactions with peroxides.
| S-EPMC1138194 | biostudies-other
Project description:1. The kinetics of formation of horseradish peroxidase Compound I were studied by using peroxobenzoic acid and ten substituted peroxobenzoic acids as substrates. Kinetic data for the formation of Compound I with H2O2 and for the reaction of deuteroferrihaem with H2O2 and peroxobenzoic acids, to form a peroxidatically active intermediate, are included for comparison. 2. The observed second-order rate constants for the formation of Compound I with peroxobenzoic acids decrease with increasing pH, in the range pH 5-10, in contrast with pH-independence of the reaction with H2O2. The results imply that the formation of Compound I involves a reaction between the enzyme and un-ionized hydroperoxide molecules. 3. The maximal rate constants for Compound I formation with unhindered peroxobenzoic acids exceed that for H2O2. Peroxobenzoic acids with bulky ortho substituents show marked adverse steric effects. The pattern of substituent effects does not agree with expectations for an electrophilic oxidation of the enzyme by peroxoacid molecules in aqueous solution, but is in agreement with that expected for a reaction involving nucleophilic attack by peroxo anions. 4. Possible reaction mechanisms are considered by which the apparent conflict between the pH-effect and substituent-effect data may be resolved. A model in which it is postulated that a negatively charged 'electrostatic gate' controls access of substrate to the active site and may also activate substrate within the active site, provides the most satisfactory explanation for both the present results and data from the literature.
| S-EPMC1163839 | biostudies-other
Project description:One important property of tannins involves their ability to form coordination compounds with metal ions, which is vital for the bioavailability of these ions, as well as for the antibacterial and antioxidative activities of tannins. In this study, the pH dependence of interactions between gallic acid, one of the basic building blocks of tannins, and Fe(II) ions, was investigated using UV/Vis spectroscopy, in conjunction with density functional theory (DFT) calculations. Moreover, two models were developed to explain the processes taking place in the solution. The first model treated the reaction as a simple bimolecular process while the second also considered the protolytic equilibrium, which was proven very successful in discerning the pH dependence of formation constants, and whose assumptions were well supported by DFT calculations. We showed that the two-time deprotonated gallic acid species forms the coordination compound with Fe(II) ions in a 1:1 molar ratio. To gain better insight into the process, the coordination compound formation was also studied using various DFT functionals, which further supported the model results. Furthermore, due to the relatively low sample amounts needed, the methodology developed here will be useful to study compounds that are more difficult to isolate.
| S-EPMC8619179 | biostudies-literature
Project description:A mechanism accounting for the robust catalase activity in catalase-peroxidases (KatG) presents a new challenge in heme protein enzymology. In Mycobacterium tuberculosis, KatG is the sole catalase and is also responsible for peroxidative activation of isoniazid, an anti-tuberculosis pro-drug. Here, optical stopped-flow spectrophotometry, rapid freeze-quench EPR spectroscopy both at the X-band and at the D-band, and mutagenesis are used to identify catalase reaction intermediates in M. tuberculosis KatG. In the presence of millimolar H2O2 at neutral pH, oxyferrous heme is formed within milliseconds from ferric (resting) KatG, whereas at pH 8.5, low spin ferric heme is formed. Using rapid freeze-quench EPR at X-band under both of these conditions, a narrow doublet radical signal with an 11 G principal hyperfine splitting was detected within the first milliseconds of turnover. The radical and the unique heme intermediates persist in wild-type KatG only during the time course of turnover of excess H2O2 (1000-fold or more). Mutation of Met255, Tyr229, or Trp107, which have covalently linked side chains in a unique distal side adduct (MYW) in wild-type KatG, abolishes this radical and the catalase activity. The D-band EPR spectrum of the radical exhibits a rhombic g tensor with dual gx values (2.00550 and 2.00606) and unique gy (2.00344) and gz values (2.00186) similar to but not typical of native tyrosyl radicals. Density functional theory calculations based on a model of an MYW adduct radical built from x-ray coordinates predict experimentally observed hyperfine interactions and a shift in g values away from the native tyrosyl radical. A catalytic role for an MYW adduct radical in the catalase mechanism of KatG is proposed.
| S-EPMC2652337 | biostudies-literature
Project description:Paper spray mass spectrometry (PS-MS) has evolved into a promising tool for monitoring reactions in thin films and microdroplets, known as reactive PS, alongside its established role in ambient and direct ionization. This study addresses the need for rapid, cost-effective methods to improve analyte identification in biofluids by leveraging reactive PS-MS in clinical chemistry environments. The technique has proven effective in derivatizing target analytes, altering hydrophobicity to enhance elution and ionization efficiency, and refining detection through thin-film reactions on paper, significantly expediting reaction rates by using amino acids (AAs) as model analytes. These molecules are prone to interacting with substrates like paper, impeding elution and detection. Additionally, highly abundant species in biofluids, such as lipids, often suppress AA ionization. This study employs the Schiff base (SB) reaction utilizing aromatic aldehydes for AA derivatization to optimize reaction conditions time, temperature, and catalyst presence and dramatically increasing the conversion ratio (CR) of formed SB. For instance, using leucine as a model AA, the CR surged from 57% at room temperature to 89% at 70 °C, with added pyridine during and after 7.5 min, displaying a 43% CR compared to the bulk reaction. Evaluation of various aromatic aldehydes as derivatization agents highlighted the importance of specific oxygen substituents for achieving higher conversion rates. Furthermore, diverse derivatization agents unveiled unique fragmentation pathways, aiding in-depth annotation of the target analyte. Successfully applied to quantify AAs in human and rat plasma, this reactive PS-MS approach showcases promising potential in efficiently detecting conventionally challenging compounds in PS-MS analysis.
| S-EPMC10993198 | biostudies-literature
Project description:Isocyanic acid, HNCO, mainly emitted by combustion processes, is doubted to be detrimental to human health if its concentration surpasses ∼1 ppbv. Very little information has been found regarding the HNCO loss in the gas phase. This study aims to close this knowledge gap by performing a theoretical kinetic study on the reaction of HNCO with the propargyl radical. The potential energy surface of the HNCO + C3H3 reaction was characterized utilizing high-level CCSD(T)/CBS(TQ5)//B3LYP/6-311++G(3df,2p) quantum-chemical approaches, followed by TST and RRKM/ME kinetic computations. The obtained results reveal that the reaction can proceed via H-abstraction, leading to the C3H4 + NCO bimolecular products with energy barriers of 23-25 kcal/mol, and/or addition, resulting in C4H4NO intermediates with 23-26 kcal/mol barrier heights. The C4H4NO adducts when formed can decompose to products and/or return to HNCO + C3H3 in which the reverse decompositions are found to be dominant with a branching ratio that accounts for nearly 100% at 300 K and 760 Torr. The calculated P-independent rate coefficients indicate that at low temperatures, the H-abstraction channels are insignificant. However, at high temperatures (T > 1500 K), the H-abstraction path leading to H3CCCH + NCO prevails with a branching ratio of ∼50-53% in the descending 1800-1500 K temperature range at 760 Torr, while the H-abstraction leading to H2CCCH2 + NCO is favorable at T > 1800 K, with the yield reaching above 50% at 760 Torr. In contrast to the H-abstraction rate constants, the calculated values for the additions and the C4H4NO decompositions show a positive pressure dependence. Both the total rate constants for the reactions HNCO + C3H3 → products and C4H4NO → products, which are, respectively, k _total_bimo(T) = 3.53 × 10-23 T 3.27 exp[(-21.35 ± 0.06 kcal/mol)/RT] cm3 molecule-1 s-1 and k _total_uni(T) = 1.13 × 1025 T -4.02 exp[(-11.77 ± 0.16 kcal/mol)/RT] s-1, increase with the increasing temperature in the 300-2000 K range at 760 Torr. The rate constant of HNCO + C3H3 → products is about 8 orders of magnitude smaller than the value of HCHO + C3H3 → products, showing that HCHO is more reactive toward the C3H3 free radicals than HNCO. The computed heats of formation for several species agree well with the available literature data with the deviation less than 1.0 kcal/mol, indicating that the methods used in this study are extremely reliable. With the given results, it is vigorously suggested that the predicted rate constants, together with the thermodynamic data of the species involved, can be confidently used for modeling HNCO-related systems under atmospheric and combustion conditions.
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Project description:Background and aimsThe use of grafted plants in vegetable crop production is now being expanded greatly. However, few data are available on the formation of graft unions in vegetables. In this work, the structural development of the graft union formation in tomato plants is studied, together with the possible relationship with activities of peroxidases and catalases.MethodsTomato (Lycopersicon esculentum Mill.) seedlings of cultivar Fanny were grafted on the rootstock of cultivar AR-9704 using the 'tongue approach grafting' method, and were grown in a crop chamber. A study of the structural development of the graft union and the involvement of peroxidases and catalases in the process of graft formation was carried out during the first stages of the graft union (4, 8 and 15 d after grafting).Key resultsObservation of the structure of the graft union showed formation of xylem and phloem vessels through the graft union 8 d after grafting. In addition, root hydraulic conductance, L0, indicate that the graft union is fully functional 8 d after grafting, which coincided with an increase of peroxidase and catalase activities.ConclusionsThese results suggest that increased peroxidase and catalase activities might be implicated in graft development in tomato plants.
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Project description:Pyridoxamine (PM) could competitively protect amino groups in proteins from glycating agents. Although PM is expected to react with saccharides, available data therein are limited. In this study, a novel hydrophilic compound from a model reaction solution containing PM and xylose was isolated and identified as (6aR,9aR)-1,8,9-trihydroxy-2,6a-dimethyl-6a,9a-dihydrocyclopenta[5,6]pyrano[3,4-c]pyridin-7(5H)-one with a tricyclic structure. This compound appeared to be specifically formed from pentose via 1-deoxypentosone, and its formation was facilitated over a pH range of 7.0-8.0. After heating at 90 °C for 5 h in a reaction mixture containing 30 mM PM and pentose at pH 7.4, this compound was obtained at a yield of 6.95-8.53 mM.
| S-EPMC7000833 | biostudies-literature
Project description:In this paper, I discuss nominal compound formation in language contact situations, the question being of how compounding in language mixing can inform both theories of mixing and theories of word-hood. This contributes to our further understanding of how word formation operates in cases of language mixing and what exactly is being mixed in mixing, i.e., words vs. units smaller than words, e.g., stems or roots. Compounding is important to answer this question, as languages differ with respect to the units they employ for compound formation, i.e., phrases vs. stems. The data to be discussed will be a mixture of materials that have already been published in the literature and newly collected data and involve several mixing varieties, namely, Greek-English, Greek-Italian, Greek-Turkish, Turkish-Norwegian, Turkish-Dutch, and French-Dutch. I then offer an analysis using the tools of syntactic models of word formation (e.g., distributed morphology), assuming a decompositional approach.
| S-EPMC7283911 | biostudies-literature