ArticleThe Journal of biological chemistry2010
Dihydroflavin-driven adenosylation of 4-coordinate Co(II) corrinoids: are cobalamin reductases enzymes or electron transfer proteins?
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- MACAW: a method for semi-automatic detection of errors in genome-scale metabolic models.Genome biology · 2025Article
- Electrochemical cofactor recycling of bacterial microcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Corrinoid salvaging and cobamide remodeling in bacteria and archaea.Journal of bacteriology · 2024Review
- Electrochemical cofactor recycling of bacterial microcompartments.bioRxiv : the preprint server for biology · 2024Article
- Coordination Chemistry Controls Coenzyme BInorganic chemistry · 2023Article
- Biosynthesis of Tetrapyrrole Cofactors by Bacterial Community Inhabiting Porphyrine-Containing Shale Rock (Fore-Sudetic Monocline).Molecules (Basel, Switzerland) · 2021Article
- Article
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- Mutational and Functional Analyses of Substrate Binding and Catalysis of theBiochemistry · 2020Article
- Review
- A New Class of EutT ATP:Co(I)rrinoid Adenosyltransferases Found in Listeria monocytogenes and Other Firmicutes Does Not Require a Metal Ion for Activity.Biochemistry · 2018Article
- Spectroscopic Study of the EutT Adenosyltransferase from Listeria monocytogenes: Evidence for the Formation of a Four-Coordinate Cob(II)alamin Intermediate.Biochemistry · 2018Article
- Resonance Raman spectroscopic study of the interaction between Co(II)rrinoids and the ATP:corrinoid adenosyltransferase PduO from Lactobacillus reuteri.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Spectroscopic Studies of the EutT Adenosyltransferase from Salmonella enterica: Mechanism of Four-Coordinate Co(II)Cbl Formation.Journal of the American Chemical Society · 2016Article
- The Crystal Structure of the C-Terminal Domain of the Salmonella enterica PduO Protein: An Old Fold with a New Heme-Binding Mode.Frontiers in microbiology · 2016Article
- Unprecedented Mechanism Employed by the Salmonella enterica EutT ATP:Co(I)rrinoid Adenosyltransferase Precludes Adenosylation of Incomplete Co(II)rrinoids.Angewandte Chemie (International ed. in English) · 2015Article
- FAD binding, cobinamide binding and active site communication in the corrin reductase (CobR).Bioscience reports · 2014Article
- Small but powerful, the primary endosymbiont of moss bugs, Candidatus Evansia muelleri, holds a reduced genome with large biosynthetic capabilities.Genome biology and evolution · 2014Article
- the Eutt enzyme of Salmonella enterica is a unique ATP:Cob(I)alamin adenosyltransferase metalloprotein that requires ferrous ions for maximal activity.Journal of bacteriology · 2014Article
- The human flavoproteome.Archives of biochemistry and biophysics · 2013Review
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2 authors.
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Abstract
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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