Redox-dependent Structural Changes in Archaeal and Bacterial Rieske-type [2Fe-2S] Clusters
Proteins containing Rieske-type [2Fe-2S] clusters play important roles in many biological electron transfer reactions. Typically, [2Fe-2S] clusters are not directly involved in the catalytic transformation of substrate, but rather supply electrons to the active site. We report herein X-ray absorption spectroscopic (XAS) data that directly demonstrate an average increase in the iron-histidine bond length of at least 0.1 {angstrom} upon reduction of two distantly related Rieske-type clusters in archaeal Rieske ferredoxin from Sulfolobus solfataricus strain P-1 and bacterial anthranilate dioxygenases from Acinetobacter sp. strain ADP1. This localized redox-dependent structural change may fine tune the protein-protein interaction (in the case of ARF) or the interdomain interaction (in AntDO) to facilitate rapid electron transfer between a lower potential Rieske-type cluster and its redox partners, thereby regulating overall oxygenase reactions in the cells.
- Research Organization:
- SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
- Sponsoring Organization:
- USDOE Office of Science (US)
- DOE Contract Number:
- AC03-76SF00515
- OSTI ID:
- 815847
- Report Number(s):
- SLAC-REPRINT-2002-252; TRN: US200319%%551
- Journal Information:
- Protein Science, Other Information: Protein Sci.11:2969,2002; PBD: 1 Jan 2002
- Country of Publication:
- United States
- Language:
- English
Similar Records
Structures of the multicomponent Rieske non-heme iron toluene 2, 3-dioxygenase enzyme system
Crystallization and preliminary X-ray analysis of the Rieske-type [2Fe–2S] ferredoxin component of biphenyl dioxygenase from Pseudomonas sp. strain KKS102