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J Biol Chem, Vol. 274, Issue 33, 23176-23184, August 13, 1999

Iron Coordination Structures of Oxygen Sensor FixL Characterized by Fe K-edge Extended X-ray Absorption Fine Structure and Resonance Raman Spectroscopy

From the Institute of Physical and Chemical Research, RIKEN Harima Institute, Mikazuki-cho, Sayo, Hyogo 679-5143, Japan

Richard W. Strange, and S. Samar Hasnain

From the Daresbury Laboratory, Warrington, Cheshire WA4 4AD, United Kingdom

FixL is a heme-based O₂ sensor protein involved in a two-component system of a symbiotic bacterium. In the present study, the iron coordination structure in the heme domain of Rhizobium meliloti FixLT (RmFixLT, a soluble truncated FixL) was examined using Fe K-edge extended x-ray absorption fine structure (EXAFS) and resonance Raman spectroscopic techniques. In the EXAFS analyses, the interatomic distances and angles of the Fe-ligand bond and the iron displacement from the heme plane were obtained for RmFixLT in the Fe²⁺, Fe²⁺O₂, Fe²⁺CO, Fe³⁺, Fe³⁺F, and Fe³⁺CN states. An apparent correlation was found between the heme-nitrogen (proximal His-194) distance in the heme domain and the phosphorylation activity of the histidine kinase domain. Comparison of the Fe-CO coordination geometry between RmFixLT and RmFixLH (heme domain of RmFixL), based on the EXAFS and Raman results, has suggested that the kinase domain directly or indirectly influences steric interaction between the iron-bound ligand and the heme pocket. Referring to the crystal structure of the heme domain of Bradyrhizobium japonicum FixL (Gong, W., Hao, B., Mansy, S. S., Gonzalez, G., Gilles-Gonzalez, M. A., and Chan, M. K. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 15177-15182), we discussed details of the iron coordination structure of RmFixLT and RmFixLH in relation to an intramolecular signal transduction mechanism in its O₂ sensing.

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