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

CHEMBL16300     N-hydroxybenzamide

Synonyms: NSC-3136, CCRIS 6046, Enamine_005424, AG-D-48150, AG-F-65736, ...
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High impact information on benzenecarbohydroxamic acid


Biological context of benzenecarbohydroxamic acid


Anatomical context of benzenecarbohydroxamic acid


Associations of benzenecarbohydroxamic acid with other chemical compounds

  • The three-dimensional structure of recombinant horseradish peroxidase in complex with BHA (benzhydroxamic acid) is the first structure of a peroxidase-substrate complex demonstrating the existence of an aromatic binding pocket [11].
  • The overall relatively weak binding of the hydroxamic acid analogues to HRPC is due to large entropic barriers (-11.3 to -37.9 eu) around neutral pH, with the distal Arg38 acting as an "entropic gate keeper". Dramatic enthalpy-entropy compensation is observed for BHA and 2-naphthohydroxamic acid binding to HRPC at pH 4 [12].
  • The specific inhibitory effect of benzhydroxamic acid on the cyanide-insensitive respiration could be reversed in whole cells of the yeast Saccharomycopsis lipolytica, by addition of Fe(III), in a way suggesting a competition between the added iron and an enzyme-bound metallic ion, both central atoms for the ligand benzhydroxamic acid [13].
  • The EPR spectra are superpositions of the spectra of two species of acyl aminoxyl radicals, i.e. the radicals Ph--C(= O)N(O.)H formed by oxidation of the parent benzohydroxamic acid, and the radical Ph--C(= O)N(O.)CH3, formed by trapping of methyl radicals [14].
  • In addition to these studies, we have found that HAO is competitively inhibited by benzohydroxamate, which is one atom shorter than HYPAH; its affinity is nearly 100-fold lower than that of the substrate, in contrast to the strong inhibition it exerts on mandelate racemase (Maurice, St. M., and Bearne, S. L. (2000) Biochemistry39, 13324-13335) [15].

Gene context of benzenecarbohydroxamic acid

  • For the v10 band, benzohydroxamic acid caused a frequency shift with HRP but not with LPO [16].
  • For example, the binding of BHA to HRPC is enthalpically driven at pH 7.0, with the H-bond to the distal Arg38 providing the largest contribution (6.74 kcal/mol) to the binding energy [12].
  • In addition, we summarize the results obtained with other inhibitors of the enzyme; for instance, polyhydroxy-substituted benzohydroxamic acid derivatives, a promising group of inhibitors of ribonucleotide reductase that was synthesized by Bart van'T Riet and investigated by our group [17].
  • In contrast, native ferric myoglobin and the benzohydroxamic acid adduct of ferric horseradish peroxidase show a strong and symmetric derivative-shaped Soret MCD signal which is indicative of hexacoordination with water and histidine axial ligands [18].

Analytical, diagnostic and therapeutic context of benzenecarbohydroxamic acid


  1. Proton re-uptake partitioning between uncoupling protein and ATP synthase during benzohydroxamic acid-resistant state 3 respiration in tomato fruit mitochondria. Jarmuszkiewicz, W., Almeida, A.M., Vercesi, A.E., Sluse, F.E., Sluse-Goffart, C.M. J. Biol. Chem. (2000) [Pubmed]
  2. Crystal structure of 3-chlorocatechol 1,2-dioxygenase key enzyme of a new modified ortho-pathway from the Gram-positive Rhodococcus opacus 1CP grown on 2-chlorophenol. Ferraroni, M., Kolomytseva, M.P., Solyanikova, I.P., Scozzafava, A., Golovleva, L.A., Briganti, F. J. Mol. Biol. (2006) [Pubmed]
  3. Involvement of cyanide-resistant respiration in cell-type proportioning during Dictyostelium development. Matsuyama, S.I., Maeda, Y. Dev. Biol. (1995) [Pubmed]
  4. Optical spectra of lactoperoxidase as a function of solvent. Zelent, B., Yano, T., Ohlsson, P.I., Smith, M.L., Paul, J., Vanderkooi, J.M. Biochemistry (2005) [Pubmed]
  5. High-pressure FTIR study of the stability of horseradish peroxidase. Effect of heme substitution, ligand binding, Ca++ removal, and reduction of the disulfide bonds. Smeller, L., Meersman, F., Fidy, J., Heremans, K. Biochemistry (2003) [Pubmed]
  6. Structure-activity relationships of benzohydroxamic acid inhibitors of ribonucleotide reductase. van't Riet, B., Kier, L.B., Elford, H.L. Journal of pharmaceutical sciences. (1980) [Pubmed]
  7. N-hydroxybenzenecarboximidic acid derivatives: a new class of nitroxyl-generating prodrugs. Lee, M.J., Shoeman, D.W., Goon, D.J., Nagasawa, H.T. Nitric Oxide (2001) [Pubmed]
  8. Metal complexes of salicylhydroxamic acid (H2Sha), anthranilic hydroxamic acid and benzohydroxamic acid. Crystal and molecular structure of [Cu(phen)2(Cl)]Cl x H2Sha, a model for a peroxidase-inhibitor complex. O'Brien, E.C., Farkas, E., Gil, M.J., Fitzgerald, D., Castineras, A., Nolan, K.B. J. Inorg. Biochem. (2000) [Pubmed]
  9. Benzohydroxamic acid induces polyspermic fertilization in the sea urchin Arbacia punctulata. Schuel, H., Schuel, R. Cell Biol. Int. Rep. (1987) [Pubmed]
  10. Kinetics of tert-butyl hydroperoxide decomposition in erythrocyte suspension. Sitozhevsky, A.V., Havalkin, I.V., Ivanov, V.V., Kondakova, I.V. Membrane & cell biology. (1997) [Pubmed]
  11. Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography. Henriksen, A., Schuller, D.J., Meno, K., Welinder, K.G., Smith, A.T., Gajhede, M. Biochemistry (1998) [Pubmed]
  12. Thermodynamic analysis of the binding of aromatic hydroxamic acid analogues to ferric horseradish peroxidase. Aitken, S.M., Turnbull, J.L., Percival, M.D., English, A.M. Biochemistry (2001) [Pubmed]
  13. Reversion by Fe(III) of the inhibition by hydroxamic acids of the cyanide-insensitive respiration in the yeast Saccharomycopsis lipolytica. Henry, M.F., Nyns, E.J. Arch. Microbiol. (1977) [Pubmed]
  14. Spin trapping of methyl radicals by the acyl nitroso compound Ph--C(= O)NO formed in the photochemical reaction between benzohydroxamic acid, dimethyl sulfoxide and hydrogen peroxide. An EPR study. Lagercrantz, C., Larsson, T. Free Radic. Res. (1994) [Pubmed]
  15. Hydroxamates as substrates and inhibitors for FMN-dependent 2-hydroxy acid dehydrogenases. Amar, D., North, P., Miskiniene, V., Cénas, N., Lederer, F. Bioorg. Chem. (2002) [Pubmed]
  16. Distinct heme-substrate interactions of lactoperoxidase probed by resonance Raman spectroscopy: difference between animal and plant peroxidases. Kitagawa, T., Hashimoto, S., Teraoka, J., Nakamura, S., Yajima, H., Hosoya, T. Biochemistry (1983) [Pubmed]
  17. The enzyme ribonucleotide reductase: target for antitumor and anti-HIV therapy. Szekeres, T., Fritzer-Szekeres, M., Elford, H.L. Critical reviews in clinical laboratory sciences. (1997) [Pubmed]
  18. Effects of cyanogen bromide modification of the distal histidine on the spectroscopic and ligand binding properties of myoglobin: magnetic circular dichroism spectroscopy as a probe of distal water ligation in ferric high-spin histidine-bound heme proteins. Bracete, A.M., Sono, M., Dawson, J.H. Biochim. Biophys. Acta (1991) [Pubmed]
  19. Solution characterisation by NMR spectroscopy of two horseradish peroxidase isoenzyme C mutants with alanine replacing either Phe142 or Phe143. Veitch, N.C., Williams, R.J., Bone, N.M., Burke, J.F., Smith, A.T. Eur. J. Biochem. (1995) [Pubmed]
  20. Mild chemical deglycosylation of horseradish peroxidase yields a fully active, homogeneous enzyme. Tams, J.W., Welinder, K.G. Anal. Biochem. (1995) [Pubmed]
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