Linked Life Data

10540861

Source:http://linkedlifedata.com/resource/pubmed/id/10540861

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1999-11-26
pubmed:abstractText
The yellow-colored compounds with the basic structural frame work of 7,8-dimethyl-10-alkylisoalloxazine are generally termed as flavins. The 10-ribityl derivative, riboflavin, is the most abundant flavin found in nature and is known as vitamin B2. Riboflavin is a precursor of the flavocoenzymes, FMN (flavin mononucleotide) and FAD (flavin adenine dinucleotide) which function as prosthetic groups of flavocoenzymes. While flavocoenzymes are usually bound noncovalently to apoproteins of flavoenzymes, covalently-bound flavocoenzymes also occur in nature, though much less often. Flavin molecules can exist in three different redox states, i.e., oxidized, one-electron reduced and two-electron reduced states, and therefore can participate in redox reactions as either one- or two-electron mediator, making the flavoenzymes extremely versatile in terms of substrate and type of reactions catalyzed. We classified flavoenzymes according to the electron-transfer process in their reductive and oxidative half-reactions and the mechanism of each class of flavoenzymes is discussed in detail.
pubmed:language
jpn
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0047-1852
pubmed:author
pubmed:issnType
Print
pubmed:volume
57
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2193-8
pubmed:dateRevised
2011-7-27
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
[Chemical and functional properties of flavin coenzymes].
pubmed:affiliation
Department of Biochemistry, Kumamoto University School of Medicine.
pubmed:publicationType
Journal Article, English Abstract, Review