Linked Life Data

8011645

Source:http://linkedlifedata.com/resource/pubmed/id/8011645

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1994-7-26
pubmed:abstractText
The Z isomers of benzaldoxime and 4-(hexyloxy)benzaldoxime were dehydrated into the corresponding nitriles in the presence of rat liver microsomes and NADPH or dithionite. Their E isomers remained unchanged under identical conditions. Alkylaldoximes, like phenylacetaldoxime and heptanaldoxime, are also dehydrated under these conditions, the alkylaldoximes being more rapidly transformed than the arylaldoximes. A genetically well-defined P450 expressed in yeast, P450 3A4, the major P450 isozyme in human liver, was also found to be catalytically active for dehydration of (Z)-benzaldoxime. All these reactions were found to be catalyzed by P450 Fe(II) as they required the use of intact microsomes in the presence of NADPH or dithionite and were strongly inhibited by O2 and CO as well as by classical P450 inhibitors. A P450 complex characterized by a Soret peak at 442 nm was detected during these reactions; its disappearance was found to be concomitant with the consumption of the aldoxime and the formation of the corresponding nitrile. (E)-benzaldoximes and all the studied ketoximes failed to give such complexes with P450 Fe(II). On the basis of these results, a possible mechanism for this new P450 reaction is proposed. It involves a P450 Fe(II)<--N(OH)=CHR complex as a key intermediate and a charge transfer from P450 Fe(II) to the aldoxime C=N bond which results in a cleavage of the aldoxime N-O bond.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7811-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Dehydration of alkyl- and arylaldoximes as a new cytochrome P450-catalyzed reaction: mechanism and stereochemical characteristics.
pubmed:affiliation
Laboratoire de Chimie et Biochimie Pharmacologiques et Toxicologiques, URA 400, Université Paris V, France.
pubmed:publicationType
Journal Article