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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2010-5-6
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pubmed:abstractText |
The free flavin-dependent Fenton reaction was detected in cell-free extracts of Chlorella. The corresponding enzyme was purified to homogeneity, and its N-terminal sequence was highly homologous to those of aldo-keto reductase family enzymes. The purified enzyme displayed aldehyde reductase activity in the presence of NADPH. Additionally, it showed ferric reductase activity and drove the Fenton reaction in the presence of free FAD and NADH.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1347-6947
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pubmed:author |
pubmed-author:AbeAkiraA,
pubmed-author:AraiToshiakiT,
pubmed-author:FusayamaKouichiK,
pubmed-author:KawasakiShinjiS,
pubmed-author:NakagawaJunichiJ,
pubmed-author:NiimuraYouichiY,
pubmed-author:NishiyamaRikaR,
pubmed-author:SatoJunichiJ,
pubmed-author:SatoTakumiT,
pubmed-author:TakedaKoujiK,
pubmed-author:WatanabeToshihiroT
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pubmed:issnType |
Electronic
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
854-7
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pubmed:meshHeading |
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pubmed:year |
2010
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pubmed:articleTitle |
Chlorella vulgaris aldehyde reductase is capable of functioning as ferric reductase and of driving the fenton reaction in the presence of free flavin.
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pubmed:affiliation |
Department of Bioscience, Tokyo University of Agriculture, Japan.
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pubmed:publicationType |
Journal Article
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