Source:http://linkedlifedata.com/resource/pubmed/id/16139790
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
2005-11-2
|
pubmed:abstractText |
Oxygen has always been recognized as an essential element of many life forms, initially through its role as a terminal electron acceptor for the energy-generating pathways of oxidative phosphorylation. In 1955, Hayaishi et al. [Mechanism of the pyrocatechase reaction, J. Am. Chem. Soc. 77 (1955) 5450-5451] presented the most important discovery that changed this simplistic view of how Nature uses atmospheric dioxygen. His discovery, the naming and mechanistic understanding of the first "oxygenase" enzyme, has provided a wonderful opportunity and scientific impetus for four decades of researchers. This volume provides an opportunity to recognize the breakthroughs of the "Hayaishi School." Notable have been the prolific contributions of Professor Ishimura et al. [Oxygen and life. Oxygenases, Oxidases and Lipid Mediators, International Congress Series, Elsevier, Amsterdam, 2002], a first-generation Hayaishi product, to characterization of the cytochrome P450 monooxygenases.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Camphor 5-Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome P-450 Enzyme System,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing),
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0006-291X
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
9
|
pubmed:volume |
338
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
346-54
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:16139790-Bacterial Proteins,
pubmed-meshheading:16139790-Camphor 5-Monooxygenase,
pubmed-meshheading:16139790-Catalysis,
pubmed-meshheading:16139790-Crystallography, X-Ray,
pubmed-meshheading:16139790-Cytochrome P-450 Enzyme System,
pubmed-meshheading:16139790-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:16139790-Heme,
pubmed-meshheading:16139790-Heme Oxygenase (Decyclizing),
pubmed-meshheading:16139790-History, 20th Century,
pubmed-meshheading:16139790-Peroxidases
|
pubmed:year |
2005
|
pubmed:articleTitle |
Thirty years of microbial P450 monooxygenase research: peroxo-heme intermediates--the central bus station in heme oxygenase catalysis.
|
pubmed:affiliation |
Department of Biochemistry, University of Illinois, Urbana, IL 61801, USA. s-sligar@uiuc.edu
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Historical Article,
Research Support, N.I.H., Extramural
|