Source:http://linkedlifedata.com/resource/pubmed/id/12418885
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
45
|
| pubmed:dateCreated |
2002-11-6
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| pubmed:abstractText |
Spin-labeled Cys89 of the soluble methane monooxygenase regulatory protein (MMOB) from Methylococcus capsulatus (Bath) binds within 15 +/- 4 A of the hydroxylase (MMOH) diiron center, placing the MMOB docking site in the MMOH "canyon" region on iron-coordinating helices E and F of the alpha-subunit.
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| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0002-7863
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
13
|
| pubmed:volume |
124
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
13392-3
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| pubmed:dateRevised |
2008-1-17
|
| pubmed:meshHeading |
pubmed-meshheading:12418885-Binding Sites,
pubmed-meshheading:12418885-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:12418885-Kinetics,
pubmed-meshheading:12418885-Methylococcus capsulatus,
pubmed-meshheading:12418885-Models, Molecular,
pubmed-meshheading:12418885-Multienzyme Complexes,
pubmed-meshheading:12418885-Oxygenases,
pubmed-meshheading:12418885-Protein Conformation
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
Component B binding to the soluble methane monooxygenase hydroxylase by saturation-recovery EPR spectroscopy of spin-labeled MMOB.
|
| pubmed:affiliation |
Department of Chemistry, Yale University, P.O. Box 208107, New Haven, Connecticut 06520-8107, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|