ReviewChembiochem : a European journal of chemical biology2010
Adenosyl radical: reagent and catalyst in enzyme reactions.
Review in Chembiochem : a European journal of chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Structure-Based Demystification of Radical Catalysis by a Coenzyme BAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Structure-Based Demystification of Radical Catalysis by a Coenzyme BAngewandte Chemie (International ed. in English) · 2022Article
- Changes in ATP Sulfurylase Activity in Response to Altered Cyanobacteria Growth Conditions.Microbes and environments · 2021Article
- Viperin: An ancient radical SAM enzyme finds its place in modern cellular metabolism and innate immunity.The Journal of biological chemistry · 2020Review
- One-carbon metabolism, folate, zinc and translation.Microbial biotechnology · 2020Article
- Targeting viperin to the mitochondrion inhibits the thiolase activity of the trifunctional enzyme complex.The Journal of biological chemistry · 2020Article
- Revisiting the methionine salvage pathway and its paralogues.Microbial biotechnology · 2019Article
- On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes.Frontiers in chemistry · 2017Review
- Does Viperin Function as a Radical S-Adenosyl-l-methionine-dependent Enzyme in Regulating Farnesylpyrophosphate Synthase Expression and Activity?The Journal of biological chemistry · 2016Article
- 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
- Probing reversible chemistry in coenzyme B12 -dependent ethanolamine ammonia lyase with kinetic isotope effects.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Glutamate 338 is an electrostatic facilitator of C-Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase.The FEBS journal · 2015Article
- Spore photoproduct lyase: the known, the controversial, and the unknown.The Journal of biological chemistry · 2015Review
- Spectroscopic studies of the Salmonella enterica adenosyltransferase enzyme SeCobA: molecular-level insight into the mechanism of substrate Cob(II)alamin activation.Biochemistry · 2014Article
- The mononuclear molybdenum enzymes.Chemical reviews · 2014Review
- Producing proficient methyl donors from alternative substrates of S-adenosylmethionine synthetase.Biochemistry · 2014Article
- Role of active site residues in promoting cobalt-carbon bond homolysis in adenosylcobalamin-dependent mutases revealed through experiment and computation.Biochemistry · 2014Article
- Dynamic, electrostatic model for the generation and control of high-energy radical intermediates by a coenzyme B₁₂-dependent enzyme.Chembiochem : a European journal of chemical biology · 2013Article
- Alternative substrates selective for S-adenosylmethionine synthetases from pathogenic bacteria.Archives of biochemistry and biophysics · 2013Article
- The enzyme-mediated direct reversal of a dithymine photoproduct in germinating endospores.International journal of molecular sciences · 2013Article
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3 authors.
Funding
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.
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