[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.-Reference-Cited by-同舟云学术

[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.

Published:1985-11 Issue:26 Volume:260 Page:14035-14044
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Arciero D M,Orville A M,Lipscomb J D

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference44 articles.

1. Molecular Mechanisms of Oxygen Activation;Nozaki,1974

2. Mössbauer and EPR spectroscopy on protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa

3. Protocatechuate 3,4-dioxygenase

4. 17O-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.

5. Raman spectral evidence for tyrosine coordination of iron in protocatechuate 3,4-dioxygenase

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