Catalase simulator

Catalase simulator PPFe0H/Al203 possesses hydroxide in the fifth coordination position of the ion. In this form, the catalyst displays high catalase and peroxidase activity (see below). 

The intermediate Fe—OOH is a mobile compound. Therefore, stereochemical diagrams show satisfactory interatomic distances and bond angles. It is obvious that the complex Fe—OOH is better adapted for two-electron reactions proceeding in one stage. Unfortunately, it has not yet been detected by spectroscopy methods because of its high activity in the reaction mentioned. There is a possibility of solving this question using catalase simulators [114, 115]. 

Worwood, M. (1990). Ferritin. Blood Rev. 4, 259-269. Yohn, J.J., Duncan, K.O., Loudon, E., Dormish, J., Repine, J.E. and Norris, D.A. (1992). Human keratinocyte catalase synthesis is decreased by simulated sunlight exposure (abstr). J. Invest. Dermatol. 98, 655A. 

The MnIIIMnIV (superoxidized) state of catalases was further subjected to several x-ray and magnetic resonance studies. The MnIIIMnIV core of L. plari-tarum was probed at three different EPR microwave frequencies, resulting in self-consistent g and A values. In turn, these parameters were used successfully to simulate both the low- and conventional frequency spectra. The EPR parameters agreed well with one another as well as with those of previous studies [88],... 

These studies simulate several of the most important functions of redox enzymes (catalases, peroxidases and monooxygenases) develop their biological simulators and explain some aspects of the action mechanism of these enzymes. 

Fita and Rossmann [100] presented a comprehensive analysis of the catalase active site and discussed probable catalytic mechanisms with the participation of acid-base catalytic groups in the redox transformations of the substrate. Figure 6.3 is a diagram of catalase redox transformation with formation of intermediate complexes A, III and IV. Note that in this work the experimentally found analogy of complex II formation for catalase and cytochrome-c-peroxidase complex is applied to particular simulations [101, 102],... 

The area between enzymatic and chemical catalyses, associated with simulation of biochemical processes by their basic parameters, is accepted as mimetic catalysis. The key aspect of the mimetic catalyst is diversity of enzyme and biomimetic function processes, which principally distinguishes the mimetic model from traditional full simulation. Based on the analysis of conformities and diversities of enzymatic and chemical catalysis, the general aspects of mimetic catalysis are discussed. An idealized model of the biomimetic catalyst and the exclusive role of the membrane in its structural organization are considered. The most important achievements in the branch of catalysis are shown, in particular, new approaches to synthesis and study of biomimetic catalase, peroxidase and monooxidases reactions. 

For the purpose of studying the effect of the inorganic matrix origin on iron protoporphyrin biomimic activity in methane oxidation to methanol the above-mentioned carriers of the acidic-basic type were used. According to data in Tables 7.4 and 7.5, mimics derived from them simultaneously simulate catalase reaction and monooxygenase function of cytochrome P-450. 

Certain forms of catalytic behavior found in biological processes are simulated by inorganic adsorbents.1 7 Carbon can act as a catalase, oxidase, peroxidase, dehydrogenase, etc. The formation of urea from ammonium carbonate solutions at the temperature of the human body in the presence of activated carbon parallels the action of various animal tissues.8... 

Luyben et al. made simulation calculations of the drying process assuming the degradation index to be the change of activity of three enzymes alkaline phosphatase in skim milk, lipase in rye, and catalase in wheat and catalase from spinach in a buffer solution [33]. They transformed general Equation 45.2 of qualitative changes (i.e., the activity change) to the form ... 

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