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February 1, 1986Journal of Biological ChemistryOpen Access

Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases.

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Authors

DAD.M. ArcieroUtah State UniversityJLJohn D. LipscombUniversity of Minnesota System

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Arciero et al. (1986) studied this question.

synapsesocial.com/papers/6a73dc056c6745e79da8bdefhttps://doi.org/10.1016/s0021-9258(17)35913-6
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment.1983 · 175 citations
  2. 2Electron paramagnetic resonance detectable states of cytochrome P-450cam1980 · 179 citations
  3. 3The metabolism of protocatechuate by Pseudomonas testosteroni1968 · 71 citations
  4. 417O-water and cyanide ligation by the active site iron of protocatechuate 3,4-dioxygenase. Evidence for displaceable ligands in the native enzyme and in complexes with inhibitors or transition state analogs.1984 · 73 citations
  5. 5[17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases.1985 · 162 citations