Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AC1L9NAV (2R,3S)-2-hydroxy-3-nitro- pentanedioic acid

Synonyms: (2R,3S)-2-hydroxy-3-nitropentanedioic acid

Werst, M.M. et al., Telser, J. et al., Lauble, H. et al.

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High impact information on Nitroisocitrate

17O ENDOR signals were observed from Hx17O (mean = 1 or 2) bound to the [4Fe-4S]1+ cluster in samples prepared with trans-aconitate and unlabeled nitroisocitrate [1].
Crystal structures of aconitase with isocitrate and nitroisocitrate bound [2].
Previous 17O ENDOR studies [Telser et al. (1986) J. Biol. Chem. 261, 4840-4846] had disclosed that Hx17O binds to the enzyme-substrate complex and also to complexes of enzyme with the substrate analogues trans-aconitate and nitroisocitrate (1-hydroxy-2-nitro-1,3-propanedicarboxylate) [3].

References

17O electron nuclear double resonance characterization of substrate binding to the [4Fe-4S]1+ cluster of reduced active aconitase. Telser, J., Emptage, M.H., Merkle, H., Kennedy, M.C., Beinert, H., Hoffman, B.M. J. Biol. Chem. (1986) [Pubmed]
Crystal structures of aconitase with isocitrate and nitroisocitrate bound. Lauble, H., Kennedy, M.C., Beinert, H., Stout, C.D. Biochemistry (1992) [Pubmed]
17O, 1H, and 2H electron nuclear double resonance characterization of solvent, substrate, and inhibitor binding to the [4Fe-4S]+ cluster of aconitase. Werst, M.M., Kennedy, M.C., Beinert, H., Hoffman, B.M. Biochemistry (1990) [Pubmed]

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