Adenosyl Radical: Reagent and Catalyst in Enzyme Reactions
dc.contributor.author | Marsh, E. Neil G. | en_US |
dc.contributor.author | Patterson, Dustin P. | en_US |
dc.contributor.author | Li, Lei | en_US |
dc.date.accessioned | 2010-04-14T20:01:51Z | |
dc.date.available | 2011-03-01T16:26:42Z | en_US |
dc.date.issued | 2010-03-22 | en_US |
dc.identifier.citation | Marsh, E. Neil G.; Patterson, Dustin P.; Li, Lei (2010). "Adenosyl Radical: Reagent and Catalyst in Enzyme Reactions." ChemBioChem 11(5): 604-621. <http://hdl.handle.net/2027.42/69165> | en_US |
dc.identifier.issn | 1439-4227 | en_US |
dc.identifier.issn | 1439-7633 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/69165 | |
dc.description.abstract | Adenosine is undoubtedly an ancient biological molecule that is a component of many enzyme cofactors: ATP, FADH, NAD(P)H, and coenzyme A, to name but a few, and, of course, of RNA. Here we present an overview of the role of adenosine in its most reactive form: as an organic radical formed either by homolytic cleavage of adenosylcobalamin (coenzyme B 12 , AdoCbl) or by single-electron reduction of S -adenosylmethionine (AdoMet) complexed to an iron–sulfur cluster. Although many of the enzymes we discuss are newly discovered, adenosine's role as a radical cofactor most likely arose very early in evolution, before the advent of photosynthesis and the production of molecular oxygen, which rapidly inactivates many radical enzymes. AdoCbl-dependent enzymes appear to be confined to a rather narrow repertoire of rearrangement reactions involving 1,2-hydrogen atom migrations; nevertheless, mechanistic insights gained from studying these enzymes have proved extremely valuable in understanding how enzymes generate and control highly reactive free radical intermediates. In contrast, there has been a recent explosion in the number of radical-AdoMet enzymes discovered that catalyze a remarkably wide range of chemically challenging reactions; here there is much still to learn about their mechanisms. Although all the radical-AdoMet enzymes so far characterized come from anaerobically growing microbes and are very oxygen sensitive, there is tantalizing evidence that some of these enzymes might be active in aerobic organisms including humans. | en_US |
dc.format.extent | 967451 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | WILEY-VCH Verlag | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Biochemistry and Biotechnology | en_US |
dc.title | Adenosyl Radical: Reagent and Catalyst in Enzyme Reactions | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055 (USA) | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055 (USA) | en_US |
dc.contributor.affiliationum | Department of Chemistry and Chemical Biology, Indiana University, Purdue University Indianapolis, Indianapolis, IN 46202 (USA) | en_US |
dc.identifier.pmid | 20191656 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/69165/1/604_ftp.pdf | |
dc.identifier.doi | 10.1002/cbic.200900777 | en_US |
dc.identifier.source | ChemBioChem | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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