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Cox, David D., Que, Lawrence. (1988) Functional models for catechol 1,2-dioxygenase. The role of the iron(III) center. Journal Of The American Chemical Society, 110 (24) 8085-8092 doi:10.1021/ja00232a021

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Reference TypeJournal (article/letter/editorial)
TitleFunctional models for catechol 1,2-dioxygenase. The role of the iron(III) center
JournalJournal Of The American Chemical Society
AuthorsCox, David D.Author
Que, Lawrence.Author
Year1988 (November)Volume110
Issue24
PublisherAmerican Chemical Society (ACS)
DOIdoi:10.1021/ja00232a021Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1428641Long-form Identifiermindat:1:5:1428641:6
GUID0
Full ReferenceCox, David D., Que, Lawrence. (1988) Functional models for catechol 1,2-dioxygenase. The role of the iron(III) center. Journal Of The American Chemical Society, 110 (24) 8085-8092 doi:10.1021/ja00232a021
Plain TextCox, David D., Que, Lawrence. (1988) Functional models for catechol 1,2-dioxygenase. The role of the iron(III) center. Journal Of The American Chemical Society, 110 (24) 8085-8092 doi:10.1021/ja00232a021
In(1988, November) Journal Of The American Chemical Society Vol. 110 (24) American Chemical Society (ACS)

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Que, Lawrence, Kolanczyk, Richard C., White, Lloyd S. (1987) Functional models for catechol 1,2-dioxygenase. Structure, reactivity, and mechanism. Journal Of The American Chemical Society, 109 (18) 5373-5380 doi:10.1021/ja00252a012
Jang, Ho G., Cox, David D., Que, Lawrence (1991) A highly reactive functional model for the catechol dioxygenases. Structure and properties of [Fe(TPA)DBC]BPh4. Journal Of The American Chemical Society, 113 (24) 9200-9204 doi:10.1021/ja00024a028
Borovik, A. S., Que, Lawrence. (1988) Models for the iron(II)iron(III) and iron(II)iron(II) forms of iron-oxo proteins. Journal Of The American Chemical Society, 110 (7) 2345-2347 doi:10.1021/ja00215a079
Que, Lawrence, Mayer, Ruth (1982) Intermediates in the reaction of catechol 1,2-dioxygenase with pyrogallol and oxygen. Journal Of The American Chemical Society, 104 (3) 875-877 doi:10.1021/ja00367a051
Fielding, Andrew J., Lipscomb, John D., Que, Lawrence (2012) Characterization of an O2Adduct of an Active Cobalt-Substituted Extradiol-Cleaving Catechol Dioxygenase. Journal Of The American Chemical Society, 134 (2) 796-799 doi:10.1021/ja2095365
Que, Lawrence, Lauffer, Randall B., Lynch, John B., Murch, Bruce P., Pyrz, Joseph W. (1987) Elucidation of the coordination chemistry of the enzyme-substrate complex of catechol 1,2-dioxygenase by NMR spectroscopy. Journal Of The American Chemical Society, 109 (18) 5381-5385 doi:10.1021/ja00252a013
Heistand, Robert H., Roe, A. Lawrence., Que, Lawrence. (1982) Dioxygenase models. Crystal structures of [N,N'-(1,2-phenylene)bis(salicylideniminato)](catecholato-O)iron(III) and .mu.-(1,4-benzenediolato-O,O')-bis[N,N'-ethylenebis(salicylideniminato)iron(III)]. Inorganic Chemistry, 21 (2) 676-681 doi:10.1021/ic00132a041
Murch, Bruce P., Boyle, Paul D., Que, Lawrence (1985) Structures of binuclear and tetranuclear iron(III) complexes as models for ferritin core formation. Journal Of The American Chemical Society, 107 (23) 6728-6729 doi:10.1021/ja00309a061
Viswanathan, Rathinam, Palaniandavar, Mallayan, Balasubramanian, Thailampillai, Muthiah, Thomas P. (1998) Functional Models for Catechol 1,2-Dioxygenase. Synthesis, Structure, Spectra, and Catalytic Activity of Certain Tripodal Iron(III) Complexes. Inorganic Chemistry, 37 (12) 2943-2951 doi:10.1021/ic970708n
Lauffer, Randall B., Heistand, Robert H., Que, Lawrence (1981) Dioxygenase model studies: reaction of oxygen with iron catecholates. Journal Of The American Chemical Society, 103 (13) 3947-3949 doi:10.1021/ja00403a066
Cox, D. D., Benkovic, S. J., Bloom, L. M., Bradley, F. C., Nelson, M. J., Que, L., Wallick, D. E. (1988) Catecholate LMCT bands as probes for the active sites of nonheme iron oxygenases. Journal Of The American Chemical Society, 110 (7) 2026-2032 doi:10.1021/ja00215a002
 
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