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Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases.
For multiple combinations of the AD orthologue (Np and Pm), reducing system (protein-based and chemical), and substrate (n-heptanal and n-octadecanal), the preparations strictly require O(2) for activity and do not support detectable hydrolytic formate production, despite having catalytic activities similar to or greater than those reported by Marsh and co-workers. Expand
Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily.
Structural comparisons reveal that HMP-P synthase is homologous to a group of adenosylcobalamin radical enzymes, which supports an evolutionary relationship between these two superfamilies. Expand
Self-sacrifice in radical S-adenosylmethionine proteins.
This review will describe the characterization of three members of the radical SAM superfamily of metalloproteins - biotin synth enzyme, lipoyl synthase, and MiaB protein - each of which has been shown to cannibalize itself during turnover. Expand
Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase.
Results of isotope-tracer experiments indicate that the aldehyde hydrogen is retained in the HCO(2)(-) and the hydrogen in the nascent methyl group of the alkane originates, at least in part, from solvent. Expand
Lipoyl synthase requires two equivalents of S-adenosyl-L-methionine to synthesize one equivalent of lipoic acid.
It is shown that the octanoylated derivative of the lipoyl-bearing subunit of the glycine cleavage system (H-protein) is also a substrate for LipA, providing further evidence that the cofactor is synthesized on its target protein. Expand
Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase.
In vitro activity of the AD from Nostoc punctiforme (Np) was shown to require a reducing system similar to the systems employed by these O(2)-utilizing di-iron enzymes, and it is shown that aldehyde cleavage by the Np AD also requires dioxygen and results in incorporation of (18)O from ( 18)O(2) into the formate product. Expand
A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing.
Several additional mutant R1s, C230SR1, and C292SR1 were shown to have activities similar to wt-R1 with both TR/TRR/NADPH and DTT, consistent with the postulate that C462 is an active site thiol. Expand
Structural Basis for Methyl Transfer by a Radical SAM Enzyme
RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site to methylate RNA. Expand
Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii.
  • S. Booker, J. Stubbe
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 15 September 1993
Initial characterization of the recombinant RTPR indicates that its properties are identical to those of the RTPR isolated from L. leichmannii, and there is no statistically significant sequence homology with the Escherichia coli reductase that requires a dinuclear-iron center and tyrosyl radical cofactor. Expand
Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide.
Lipoyl synthase from Escherichia coli can accommodate two [4Fe-4S] clusters per polypeptide and that this form of the enzyme is relevant to turnover, and Mössbauer spectroscopy of the as-isolated wild-type protein and the two triple variants indicates that greater than 90% of all associated iron is in the configuration [4 Fe- 4S](2+). Expand