Showing papers by "Randall B. Lauffer published in 1983"
102 citations
TL;DR: Analyses of chemical shifts and the temperature dependence of the paramagnetically shifted resonances indicate that the Fe(III)-Fe(II) cluster in the reduced protein exhibits weak antiferromagnetic exchange coupling, in agreement with the estimate derived from the temperature dependent of the EPR signal intensity.
88 citations
01 Jan 1983
TL;DR: Based on NMR studies of model monodentate and chelated catecholate complexes, the substrate is shown to be coordinated to the ferric center through only one oxygen in the catechol 1, 2-dioxygenase-4-methylcatechol complex.
Abstract: Investigations into the enzyme-substrate complex of the catechol dioxygenases have vaised the possibility that the catechol may bind to the metal center in a monodentate configuration. Based on NMR studies of model monodentate and chelated catecholate complexes, the substrate is shown to be coordinated to the ferric center through only one oxygen in the catechol 1, 2-dioxygenase-4-methylcatechol complex. Rationalizations for this preferred configuration are suggested by the oxygen reactivity of various model Compounds.
1 citations