rdf:type |
|
lifeskim:mentions |
umls-concept:C0001721,
umls-concept:C0007292,
umls-concept:C0015858,
umls-concept:C0030012,
umls-concept:C0032098,
umls-concept:C0150312,
umls-concept:C0599871,
umls-concept:C0871161,
umls-concept:C1167622,
umls-concept:C1710236,
umls-concept:C1749467
|
pubmed:issue |
21
|
pubmed:dateCreated |
2004-10-29
|
pubmed:abstractText |
Substrate-free Delta9-18:0-acyl carrier protein desaturase (abbreviated to Des)[E.C. # 1.14.99.6] was 2-electron reduced with E'0=-0.03 +-0.01 V; the presence of spinach ferredoxin (SpFd) induces an additional 1-electron reduction wave at E'0=-0.21 +-0.02 V, which shifts by 0.106 V upon substrate binding.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Nov
|
pubmed:issn |
1359-7345
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
7
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2406-7
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
|
pubmed:year |
2004
|
pubmed:articleTitle |
Substrate binding and the presence of ferredoxin affect the redox properties of the soluble plant Delta9-18:0-acyl carrier protein desaturase.
|
pubmed:affiliation |
Biotechnology Division, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA. vytas@nist.gov
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
|