Photochemically driven models of oxygenases based on the use of iron porphyrins
Photoexcited iron porphyrins can be used to mimic the catalytic activity of cytochrome P-450 oxygenases both in the reduction of halogenated alkanes and in the oxidation of hydrocarbons by O2 itself at room temperature and atmospheric pressure. The results reported indicate that there is a similarit...
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Veröffentlicht in: | Journal of biological inorganic chemistry 1999-04, Vol.4 (2), p.154-161 |
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creator | Maldotti, A Andreotti, L Molinari, A Carassiti, V |
description | Photoexcited iron porphyrins can be used to mimic the catalytic activity of cytochrome P-450 oxygenases both in the reduction of halogenated alkanes and in the oxidation of hydrocarbons by O2 itself at room temperature and atmospheric pressure. The results reported indicate that there is a similarity and a complementarity of photonic activation with other more conventional methods of activation of model systems of oxygenases. In fact, by irradiating at suitable wavelengths, it is possible to induce redox reactions which mimic those of natural oxygenases, avoiding the difficulties caused by parallel processes which could be expected when chemical reagents are used. These processes occur with good turnover values of the photocatalyst and in mild temperature and pressure conditions. By controlling the reaction environment, it is possible to address the selectivity of the process. In this regard, the very recent results obtained after heterogenization of the photocatalysts inside membranes of Nafion are particularly promising for the development of new biomimetic photocatalysts in heterogeneous or organized systems. |
doi_str_mv | 10.1007/s007750050298 |
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The results reported indicate that there is a similarity and a complementarity of photonic activation with other more conventional methods of activation of model systems of oxygenases. In fact, by irradiating at suitable wavelengths, it is possible to induce redox reactions which mimic those of natural oxygenases, avoiding the difficulties caused by parallel processes which could be expected when chemical reagents are used. These processes occur with good turnover values of the photocatalyst and in mild temperature and pressure conditions. By controlling the reaction environment, it is possible to address the selectivity of the process. 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The results reported indicate that there is a similarity and a complementarity of photonic activation with other more conventional methods of activation of model systems of oxygenases. In fact, by irradiating at suitable wavelengths, it is possible to induce redox reactions which mimic those of natural oxygenases, avoiding the difficulties caused by parallel processes which could be expected when chemical reagents are used. These processes occur with good turnover values of the photocatalyst and in mild temperature and pressure conditions. By controlling the reaction environment, it is possible to address the selectivity of the process. In this regard, the very recent results obtained after heterogenization of the photocatalysts inside membranes of Nafion are particularly promising for the development of new biomimetic photocatalysts in heterogeneous or organized systems.</description><subject>Animals</subject><subject>Catalysis</subject><subject>Humans</subject><subject>Models, Chemical</subject><subject>Oxygenases - metabolism</subject><subject>Photochemistry</subject><subject>Porphyrins - metabolism</subject><issn>0949-8257</issn><issn>1432-1327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkL1PwzAQxS0EoqUwsiJPbAF_xLE9oooCUqUywBwl8ZkEJXGwE0T-e1y1Ayzv9HQ_vTs9hK4puaOEyPsQRQpCBGFanaAlTTlLKGfyFC2JTnWimJALdBHCJyGECyrO0YKSVGuixBLtXms3uqqGrqmKtp2x8c039LhzBtqAncXuZ_6AvggQcBnVYNfjsQY8BdivGx_94PxQz77pwyU6s0Ub4Oo4V-h98_i2fk62u6eX9cM2qZjSY5LxsqA6k1XGhQSmqVHxJys5K5U0qSLRijQDawpLNVM2pSJjJdWlsaU2iq_Q7SF38O5rgjDmXRMqaNuiBzeFXBKpsnghgskBrLwLwYPNB990hZ9zSvJ9g_m_BiN_cwyeyg7MH_pQGf8FDihrKA</recordid><startdate>19990401</startdate><enddate>19990401</enddate><creator>Maldotti, A</creator><creator>Andreotti, L</creator><creator>Molinari, A</creator><creator>Carassiti, V</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19990401</creationdate><title>Photochemically driven models of oxygenases based on the use of iron porphyrins</title><author>Maldotti, A ; Andreotti, L ; Molinari, A ; Carassiti, V</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c289t-63ba1967c6357e291d8104f732b87d480810546efdaf1928f41562b19bdfb9d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Catalysis</topic><topic>Humans</topic><topic>Models, Chemical</topic><topic>Oxygenases - metabolism</topic><topic>Photochemistry</topic><topic>Porphyrins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Maldotti, A</creatorcontrib><creatorcontrib>Andreotti, L</creatorcontrib><creatorcontrib>Molinari, A</creatorcontrib><creatorcontrib>Carassiti, V</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biological inorganic chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Maldotti, A</au><au>Andreotti, L</au><au>Molinari, A</au><au>Carassiti, V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Photochemically driven models of oxygenases based on the use of iron porphyrins</atitle><jtitle>Journal of biological inorganic chemistry</jtitle><addtitle>J Biol Inorg Chem</addtitle><date>1999-04-01</date><risdate>1999</risdate><volume>4</volume><issue>2</issue><spage>154</spage><epage>161</epage><pages>154-161</pages><issn>0949-8257</issn><eissn>1432-1327</eissn><abstract>Photoexcited iron porphyrins can be used to mimic the catalytic activity of cytochrome P-450 oxygenases both in the reduction of halogenated alkanes and in the oxidation of hydrocarbons by O2 itself at room temperature and atmospheric pressure. 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subjects | Animals Catalysis Humans Models, Chemical Oxygenases - metabolism Photochemistry Porphyrins - metabolism |
title | Photochemically driven models of oxygenases based on the use of iron porphyrins |
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