Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
36
|
pubmed:dateCreated |
1993-10-14
|
pubmed:abstractText |
Biological reductive dehalogenation reactions are important in environmental detoxification of organohalides. Only scarce information is available on the enzymology underlying these reactions. Cytochrome P450CAM with a known X-ray structure and well-studied oxygenase reaction cycle, has been studied for its ability to reduce carbon-halogen bonds under anaerobic conditions. The reductive reactions functioned with NADH and the physiological electron-transfer proteins or by using artificial electron donors to reduce cytochrome P450CAM. Halogenated methane and ethane substrates were transformed by a two-electron reduction and subsequent protonation, beta-elimination, or alpha-elimination to yield alkanes, alkene, or carbene-derived products, respectively. Halogenated substrates bound to the camphor binding site as indicated by saturable changes in the Fe(III)-heme spin state upon substrate addition. Hexachloromethane was bound with a dissociation constant (KD) of 0.7 microM and caused > 95% shift from low- to high-spin iron. Ethanes bearing fewer chlorine substituents were bound with increasing dissociation constants and gave lesser degrees of iron spin-state change. Camphor competitively inhibited hexachloroethane reduction with an inhibitor constant (KI) similar to the dissociation constant for camphor (KI = KD = 0.9 microM). Rate determinations with pentachloroethane indicated a 100-fold higher enzyme V/K compared to the second-order rate constant for hematin free in solution. These studies on substrate binding and catalysis will help reveal how biological systems enzymatically reduce carbon-halogen bonds in the environment.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Camphor 5-Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Dioxide,
http://linkedlifedata.com/resource/pubmed/chemical/Chlorofluorocarbons, Methane,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrocarbons, Halogenated,
http://linkedlifedata.com/resource/pubmed/chemical/Mixed Function Oxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/trichlorofluoromethane
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0006-2960
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
14
|
pubmed:volume |
32
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
9355-61
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:8369306-Camphor 5-Monooxygenase,
pubmed-meshheading:8369306-Carbon Dioxide,
pubmed-meshheading:8369306-Catalysis,
pubmed-meshheading:8369306-Chlorofluorocarbons, Methane,
pubmed-meshheading:8369306-Cytochrome P-450 Enzyme System,
pubmed-meshheading:8369306-Electron Transport,
pubmed-meshheading:8369306-Heme,
pubmed-meshheading:8369306-Hydrocarbons, Halogenated,
pubmed-meshheading:8369306-Kinetics,
pubmed-meshheading:8369306-Mixed Function Oxygenases,
pubmed-meshheading:8369306-NAD,
pubmed-meshheading:8369306-Oxidation-Reduction,
pubmed-meshheading:8369306-Pseudomonas putida,
pubmed-meshheading:8369306-Substrate Specificity
|
pubmed:year |
1993
|
pubmed:articleTitle |
Reductive dehalogenation by cytochrome P450CAM: substrate binding and catalysis.
|
pubmed:affiliation |
Department of Biochemistry, University of Minnesota, St. Paul 55108.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|