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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
2010-1-25
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pubmed:abstractText |
The identity of the source of the biological reductant needed to convert cobalamin to its biologically active form adenosylcobalamin has remained elusive. Here we show that free or protein-bound dihydroflavins can serve as the reductant of Co(2+)Cbl bound in the active site of PduO-type ATP-dependent corrinoid adenosyltransferase enzymes. Free dihydroflavins (dihydroriboflavin, FMNH(2), and FADH(2)) effectively drove the adenosylation of Co(2+)Cbl by the human and bacterial PduO-type enzymes at very low concentrations (1 microm). These data show that adenosyltransferase enzymes lower the thermodynamic barrier of the Co(2+) --> Co(+) reduction needed for the formation of the unique organometalic Co-C bond of adenosylcobalamin. Collectively, our in vivo and in vitro data suggest that cobalamin reductases identified thus far are most likely electron transfer proteins, not enzymes.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-10564814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-10873547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-10894741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-10978155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-11196321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-11408479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-12195810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-12923081,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-14729683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-14888646,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-15291577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-15317775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-15347655,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-15547259,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-15741334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-15817784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-15913339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-15954777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-16207720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-16636051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-17121823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-17543538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-18221906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-18241886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-18263579,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-18295882,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-18452306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-18672897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-19236001,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-2403541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-2857503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-4390543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-4874308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-7860601,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-8407805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-9250993,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19933577-9711234
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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:month |
Jan
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pubmed:issn |
1083-351X
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
29
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2911-7
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pubmed:dateRevised |
2011-7-20
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pubmed:meshHeading |
pubmed-meshheading:19933577-Adenosine,
pubmed-meshheading:19933577-Alkyl and Aryl Transferases,
pubmed-meshheading:19933577-Bacterial Proteins,
pubmed-meshheading:19933577-Carbon,
pubmed-meshheading:19933577-Catalytic Domain,
pubmed-meshheading:19933577-Cloning, Molecular,
pubmed-meshheading:19933577-Cobalt,
pubmed-meshheading:19933577-Corrinoids,
pubmed-meshheading:19933577-Dose-Response Relationship, Drug,
pubmed-meshheading:19933577-Electrons,
pubmed-meshheading:19933577-Flavins,
pubmed-meshheading:19933577-Humans,
pubmed-meshheading:19933577-Kinetics,
pubmed-meshheading:19933577-Oxidation-Reduction,
pubmed-meshheading:19933577-Thermodynamics,
pubmed-meshheading:19933577-Vitamin B 12
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pubmed:year |
2010
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pubmed:articleTitle |
Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins?
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pubmed:affiliation |
Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53726-1521, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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