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Title: S -Adenosyl- l -ethionine is a Catalytically Competent Analog of S -Adenosyl- l -methionine (SAM) in the Radical SAM Enzyme HydG

Journal Article · · Angewandte Chemie (International Edition)

Not provided.

Research Organization:
Montana State Univ., Bozeman, MT (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
DOE Contract Number:
SC0005404
OSTI ID:
1850936
Journal Information:
Angewandte Chemie (International Edition), Vol. 60, Issue 9; ISSN 1433-7851
Publisher:
Wiley
Country of Publication:
United States
Language:
English

References (44)

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Expanding the Chemistry of the Class C Radical SAM Methyltransferase NosN by Using an Allyl Analogue of SAM journal May 2018
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Monovalent Cation Activation of the Radical SAM Enzyme Pyruvate Formate-Lyase Activating Enzyme journal August 2017
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Radical SAM Enzyme HydE Generates Adenosylated Fe(I) Intermediates En Route to the [FeFe]-Hydrogenase Catalytic H-Cluster journal May 2020
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Mechanism of Radical Initiation in the Radical S -Adenosyl- l -methionine Superfamily journal October 2018
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A [4Fe–4S]-Fe(CO)(CN)-l-cysteine intermediate is the first organometallic precursor in [FeFe] hydrogenase H-cluster bioassembly journal April 2018
Synthesis of the 2Fe subcluster of the [FeFe]-hydrogenase H cluster on the HydF scaffold journal May 2010
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The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN ligated iron cofactor journal December 2009

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