[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

D. M. Arciero, A. M. Orville, J. D. Lipscomb

Research output: Contribution to journal › Article

138 Citations (Scopus)
Original languageEnglish (US)
Pages (from-to)14035-14044
Number of pages10
JournalJournal of Biological Chemistry
Volume260
Issue number26
StatePublished - Jan 1 1985

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Catechol 2,3-Dioxygenase
Oxygen Isotopes
Electron spin resonance spectroscopy
Oxygenases
Electron Spin Resonance Spectroscopy
Pseudomonas
Catalytic Domain
Nitric Oxide
Iron
Binding Sites
Ligands
Water
protocatechuate 4,5-dioxygenase
extradiol dioxygenase

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[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. / Arciero, D. M.; Orville, A. M.; Lipscomb, J. D.

In: Journal of Biological Chemistry, Vol. 260, No. 26, 01.01.1985, p. 14035-14044.

Research output: Contribution to journal › Article

Arciero, DM, Orville, AM & Lipscomb, JD 1985, '[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', Journal of Biological Chemistry, vol. 260, no. 26, pp. 14035-14044.
Arciero DM, Orville AM, Lipscomb JD. [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. Journal of Biological Chemistry. 1985 Jan 1;260(26):14035-14044.
Arciero, D. M. ; Orville, A. M. ; Lipscomb, J. D. / [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. In: Journal of Biological Chemistry. 1985 ; Vol. 260, No. 26. pp. 14035-14044.
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