Linked Life Data

7947938

Source:http://linkedlifedata.com/resource/pubmed/id/7947938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-12-22
pubmed:abstractText
Cytochrome P-450BM-3 from Bacillus megaterium is a soluble, catalytically self-sufficient fatty acid mono-oxygenase that resembles the Class II P-450 systems of the eukaryotic endoplasmic reticulum. Its single polypeptide chain contains both a P-450 heme domain and an NADPH:P-450 reductase domain, each of which bears significant structural and functional homology with its microsomal counterparts. We report here that cytochrome c, which can accept NADPH-derived electrons from the reductase domain of P-450-BM-3, did not inhibit myristate hydroxylation catalyzed by P-450BM-3 or by two reductase domain mutant enzymes (W574Y, W574F) which have diminished hydroxylase activity relative to wild-type enzyme but retain cytochrome c reductase activity levels comparable to wild-type enzyme. Because reduced cytochrome c generated independently of the reductase domain of P-450BM-3 did not support myristate hydroxylation, it seems likely that cytochrome c binds to a site on the reductase domain which does not overlap the site of the heme domain interaction. We also found that myristate did not inhibit P-450BM-3-mediated cytochrome c reduction. Since neither substrate inhibited the conversion of the other, we conclude that the rate-limiting steps for both myristate hydroxylation and cytochrome c reduction by P-450BM-3 do not involve electron transfer through the reductase domain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
1201
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
245-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
The interaction of cytochrome c and the heme domain of cytochrome P-450BM-3 with the reductase domain of cytochrome P-450BM-3.
pubmed:affiliation
Department of Biological Chemistry, UCLA School of Medicine.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.