Water oxidation by a cytochrome p450: mechanism and function of the reaction
P450(cam) (CYP101A1) is a bacterial monooxygenase that is known to catalyze the oxidation of camphor, the first committed step in camphor degradation, with simultaneous reduction of oxygen (O2). We report that P450(cam) catalysis is controlled by oxygen levels: at high O2 concentration, P450(cam) ca...
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| description | P450(cam) (CYP101A1) is a bacterial monooxygenase that is known to catalyze the oxidation of camphor, the first committed step in camphor degradation, with simultaneous reduction of oxygen (O2). We report that P450(cam) catalysis is controlled by oxygen levels: at high O2 concentration, P450(cam) catalyzes the known oxidation reaction, whereas at low O2 concentration the enzyme catalyzes the reduction of camphor to borneol. We confirmed, using (17)O and (2)H NMR, that the hydrogen atom added to camphor comes from water, which is oxidized to hydrogen peroxide (H2O2). This is the first time a cytochrome P450 has been observed to catalyze oxidation of water to H2O2, a difficult reaction to catalyze due to its high barrier. The reduction of camphor and simultaneous oxidation of water are likely catalyzed by the iron-oxo intermediate of P450(cam) , and we present a plausible mechanism that accounts for the 1:1 borneol:H2O2 stoichiometry we observed. This reaction has an adaptive value to bacteria that express this camphor catabolism pathway, which requires O2, for two reasons: 1) the borneol and H2O2 mixture generated is toxic to other bacteria and 2) borneol down-regulates the expression of P450(cam) and its electron transfer partners. Since the reaction described here only occurs under low O2 conditions, the down-regulation only occurs when O2 is scarce. |
| doi_str_mv | 10.1371/journal.pone.0061897 |
| format | Article |
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We report that P450(cam) catalysis is controlled by oxygen levels: at high O2 concentration, P450(cam) catalyzes the known oxidation reaction, whereas at low O2 concentration the enzyme catalyzes the reduction of camphor to borneol. We confirmed, using (17)O and (2)H NMR, that the hydrogen atom added to camphor comes from water, which is oxidized to hydrogen peroxide (H2O2). This is the first time a cytochrome P450 has been observed to catalyze oxidation of water to H2O2, a difficult reaction to catalyze due to its high barrier. The reduction of camphor and simultaneous oxidation of water are likely catalyzed by the iron-oxo intermediate of P450(cam) , and we present a plausible mechanism that accounts for the 1:1 borneol:H2O2 stoichiometry we observed. This reaction has an adaptive value to bacteria that express this camphor catabolism pathway, which requires O2, for two reasons: 1) the borneol and H2O2 mixture generated is toxic to other bacteria and 2) borneol down-regulates the expression of P450(cam) and its electron transfer partners. Since the reaction described here only occurs under low O2 conditions, the down-regulation only occurs when O2 is scarce.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0061897</identifier><identifier>PMID: 23634216</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acids ; Bacteria ; Biodegradation ; Biology ; Biomechanical Phenomena ; Bornanes - metabolism ; Borneol ; Camphor ; Camphor - metabolism ; Catabolism ; Catalysis ; Chemistry ; Cytochrome ; Cytochrome P-450 Enzyme System - chemistry ; Cytochrome P-450 Enzyme System - metabolism ; Cytochrome P450 ; Electron transfer ; Enzymes ; Gene Expression Regulation, Enzymologic ; Hydrogen ; Hydrogen atoms ; Hydrogen ion concentration ; Hydrogen peroxide ; Hydrogen Peroxide - metabolism ; Iron ; Models, Molecular ; Monooxygenase ; NMR ; Nuclear magnetic resonance ; Oxidation ; Oxidation-Reduction ; Oxidation-reduction reactions ; Oxygen ; Protein Conformation ; Pseudomonas putida ; Reduction ; Stoichiometry ; Water - metabolism</subject><ispartof>PloS one, 2013-04, Vol.8 (4), p.e61897</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Prasad et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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We report that P450(cam) catalysis is controlled by oxygen levels: at high O2 concentration, P450(cam) catalyzes the known oxidation reaction, whereas at low O2 concentration the enzyme catalyzes the reduction of camphor to borneol. We confirmed, using (17)O and (2)H NMR, that the hydrogen atom added to camphor comes from water, which is oxidized to hydrogen peroxide (H2O2). This is the first time a cytochrome P450 has been observed to catalyze oxidation of water to H2O2, a difficult reaction to catalyze due to its high barrier. The reduction of camphor and simultaneous oxidation of water are likely catalyzed by the iron-oxo intermediate of P450(cam) , and we present a plausible mechanism that accounts for the 1:1 borneol:H2O2 stoichiometry we observed. This reaction has an adaptive value to bacteria that express this camphor catabolism pathway, which requires O2, for two reasons: 1) the borneol and H2O2 mixture generated is toxic to other bacteria and 2) borneol down-regulates the expression of P450(cam) and its electron transfer partners. Since the reaction described here only occurs under low O2 conditions, the down-regulation only occurs when O2 is scarce.</description><subject>Acids</subject><subject>Bacteria</subject><subject>Biodegradation</subject><subject>Biology</subject><subject>Biomechanical Phenomena</subject><subject>Bornanes - metabolism</subject><subject>Borneol</subject><subject>Camphor</subject><subject>Camphor - metabolism</subject><subject>Catabolism</subject><subject>Catalysis</subject><subject>Chemistry</subject><subject>Cytochrome</subject><subject>Cytochrome P-450 Enzyme System - chemistry</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>Cytochrome P450</subject><subject>Electron transfer</subject><subject>Enzymes</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Hydrogen</subject><subject>Hydrogen atoms</subject><subject>Hydrogen ion concentration</subject><subject>Hydrogen peroxide</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Iron</subject><subject>Models, Molecular</subject><subject>Monooxygenase</subject><subject>NMR</subject><subject>Nuclear magnetic resonance</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Oxidation-reduction reactions</subject><subject>Oxygen</subject><subject>Protein Conformation</subject><subject>Pseudomonas putida</subject><subject>Reduction</subject><subject>Stoichiometry</subject><subject>Water - 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We report that P450(cam) catalysis is controlled by oxygen levels: at high O2 concentration, P450(cam) catalyzes the known oxidation reaction, whereas at low O2 concentration the enzyme catalyzes the reduction of camphor to borneol. We confirmed, using (17)O and (2)H NMR, that the hydrogen atom added to camphor comes from water, which is oxidized to hydrogen peroxide (H2O2). This is the first time a cytochrome P450 has been observed to catalyze oxidation of water to H2O2, a difficult reaction to catalyze due to its high barrier. The reduction of camphor and simultaneous oxidation of water are likely catalyzed by the iron-oxo intermediate of P450(cam) , and we present a plausible mechanism that accounts for the 1:1 borneol:H2O2 stoichiometry we observed. This reaction has an adaptive value to bacteria that express this camphor catabolism pathway, which requires O2, for two reasons: 1) the borneol and H2O2 mixture generated is toxic to other bacteria and 2) borneol down-regulates the expression of P450(cam) and its electron transfer partners. Since the reaction described here only occurs under low O2 conditions, the down-regulation only occurs when O2 is scarce.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23634216</pmid><doi>10.1371/journal.pone.0061897</doi><tpages>e61897</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acids Bacteria Biodegradation Biology Biomechanical Phenomena Bornanes - metabolism Borneol Camphor Camphor - metabolism Catabolism Catalysis Chemistry Cytochrome Cytochrome P-450 Enzyme System - chemistry Cytochrome P-450 Enzyme System - metabolism Cytochrome P450 Electron transfer Enzymes Gene Expression Regulation, Enzymologic Hydrogen Hydrogen atoms Hydrogen ion concentration Hydrogen peroxide Hydrogen Peroxide - metabolism Iron Models, Molecular Monooxygenase NMR Nuclear magnetic resonance Oxidation Oxidation-Reduction Oxidation-reduction reactions Oxygen Protein Conformation Pseudomonas putida Reduction Stoichiometry Water - metabolism |
| title | Water oxidation by a cytochrome p450: mechanism and function of the reaction |
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