Send to

Choose Destination
Biochemistry. 1989 Sep 5;28(18):7233-40.

X-ray absorption spectroscopy of the [2Fe-2S] Rieske cluster in Pseudomonas cepacia phthalate dioxygenase. Determination of core dimensions and iron ligation.

Author information

Department of Chemistry, University of Michigan, Ann Arbor 48109-1055.


We have employed X-ray absorption spectroscopy to obtain structural information about the Rieske Fe/S center in the phthalate dioxygenase (PDO) from Pseudomonas cepacia. Native PDO contains a dinuclear Rieske Fe/S center and an additional mononuclear Fe site. In order to study selectively the Fe/S cluster, we measured data for samples in which the mononuclear site was either depleted of metal or reconstituted with Co or Zn. Our results demonstrate that the iron environment in the Rieske cluster is structurally indistinguishable from that found in other Fe/S clusters, thus strongly supporting the suggestion that the unusually high reduction potentials for Rieske clusters are due to electrostatic rather than structural effects. The average Fe-Fe distance is 2.68 (3) A for both oxidized and reduced Rieske clusters. The average Fe-S distance is 2.24 (2) A in the oxidized cluster and 2.28 (2) A in the reduced cluster. Careful analysis of the EXAFS Debye-Waller factors suggests that the bridging and terminal Fe-S distances for the oxidized cluster are 2.20 and 2.31 A, respectively. Taken together with recent ENDOR results, these studies provide a detailed structural model for the Rieske [2Fe-2S] centers.

[Indexed for MEDLINE]

Supplemental Content

Loading ...
Support Center