A ligand field model for MCD spectra of biological cupric complexes.

A ligand field calculation of magnetic circular dichroism (MCD) spectra is described that provides new insights into the information contained in electronic spectra of copper sites in metalloenzymes and synthetic analogs. The ligand field model uses metal-centered p- and f-orbitals to model sigma, pi LMCT mixing mechanism for intensity, allowing the basic features of optical absorption, MCD, and electron paramagnetic resonance spectra to be simultaneously computed from a single set of parameters and the crystallographically determined ligand coordinates. We have used the model to predict changes in spectra resulting from the transformation of electronic wavefunctions under systematic variation in geometry in pentacoordinate ML5 complexes. The effectiveness of the calculation is demonstrated for two synthetic copper model compounds and a galactose oxidase enzyme complex representing limiting coordination geometries. This analysis permits immediate recognition of characteristic patterns of MCD intensity and correlation with geometry. A complementarity principle between MCD and CD spectra of transition metal complexes is discussed.

Magnetic circular dichroism studies on the mononuclear ferrous active site of phthalate dioxygenase from Pseudomonas cepacia show a change of ligation state on substrate binding.

Phthalate dioxygenase from Pseudomonas cepacia contains a mononuclear ferrous center that is strictly required for catalytic oxygen activation. The spectroscopic characterization of this iron site and its ligand interactions has been complicated in the past by interference from a Rieske-type binuclear (2Fe-2S) cluster in the enzyme, which dominates the absorption spectra and is superimposed in X-ray absorption spectra for the mononuclear site. We have used low-temperature, variable magnetic field circular dichroism spectroscopy to selectively detect the ligand field spectra of the paramagnetic mononuclear ferrous active site in the presence of the diamagnetic exchange-coupled Rieske center and observe spectral changes associated with substrate binding. The perturbations of the d-->d spectra for the mononuclear ferrous site reflect a decrease in coordination number from six to five on binding substrate. This structural change suggests that displacement of an iron ligand prepares the ferrous center for dioxygen activation.