Oxygen-independent decarbonylation of aldehydes by cyanobacterial aldehyde decarbonylase: a new reaction of diiron enzymes.

@article{Das2011OxygenindependentDO,
  title={Oxygen-independent decarbonylation of aldehydes by cyanobacterial aldehyde decarbonylase: a new reaction of diiron enzymes.},
  author={Debasis Das and B. Eser and Jaehong Han and Aaron Sciore and E. Marsh},
  journal={Angewandte Chemie},
  year={2011},
  volume={50 31},
  pages={
          7148-52
        }
}
The search for new biofuels has generated increased interest in biochemical pathways that produce hydrocarbons.[1] Although hydrocarbons are simple molecules, the biosynthesis of molecules that lack any chemical functional groups is surprisingly challenging.[2] Biochemical reactions that remove functionality, such as decarboxylations, dehydrations and reduction of double bonds, invariably rely on the presence of adjacent functional groups to stabilize unfavorable transition states. Enzymes… Expand
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References

SHOWING 1-10 OF 35 REFERENCES
Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase.
TLDR
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
Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase.
TLDR
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
Alkane biosynthesis by decarbonylation of aldehydes catalyzed by a particulate preparation from Pisum sativum.
TLDR
It is concluded that the aldehydes produced by the acyl-CoA reductase located in the endomembranes of the epidermal cells are converted to alkanes by the decarbonylase Located in the cell wall/cuticle region. Expand
Exotic biomodification of fatty acids.
  • P. H. Buist
  • Chemistry, Medicine
  • Natural product reports
  • 2007
TLDR
This review highlights the bioorganic aspects of selected reactions of mid- to long chain fatty acyl derivatives that lead to a diverse array of bioactive compounds. Expand
Mechanistic studies on the hydroxylation of methane by methane monooxygenase.
TLDR
Methanotrophs are bacteria that live on methane as their only source of carbon and the first step in their utilization is its selective conversion to methanol, which in turn is processed into biomass. Expand
Oxygen activating nonheme iron enzymes.
  • S. Lange, L. Que
  • Chemistry, Medicine
  • Current opinion in chemical biology
  • 1998
TLDR
Synthetic complexes have successfully mimicked chemistry performed by both mono- and dinuclear nonheme iron enzymes, such as the extradiol-cleaving catechol dioxygenases, lipoxygenase, alkane and alkene monoxygenases and fatty acid desaturases. Expand
A cobalt-porphyrin enzyme converts a fatty aldehyde to a hydrocarbon and CO.
  • M. Dennis, P. Kolattukudy
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1992
TLDR
The results strongly suggest that biosynthesis of hydrocarbons is effected by a microsomal Co-porphyrin-containing enzyme that catalyzes decarbonylation of aldehydes and, thus, reveal a biological function for Co in plants. Expand
An allylic ketyl radical intermediate in clostridial amino-acid fermentation
TLDR
This work identifies a kinetically competent product-related allylic ketyl radical bound to the enzyme by electron paramagnetic resonance spectroscopy employing isotope-labelled (R)-2-hydroxy-4-methylpentanoyl-CoA species and finds that the enzyme generated the stabilized pentadienoyl ketylradical from the substrate analogue 2-hydroxypent- 4-enoyl -CoA, supporting the proposed mechanism. Expand
Ribonucleotide reductases — a group of enzymes with different metallosites and a similar reaction mechanism
Ribonucleotide reductases catalyze an essential reaction in all living cells — the production of deoxyribonucleotide precursors for DNA synthesis. An intricate allosteric regulation enables one andExpand
Adenosyl Radical: Reagent and Catalyst in Enzyme Reactions
TLDR
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. Expand
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