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J. Biol. Chem., Vol. 279, Issue 50, 51981-51988, December 10, 2004

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The Interaction of Covalently Bound Heme with the Cytochrome c Maturation Protein CcmE^*

Takeshi Uchida, Julie M. Stevens¶, Oliver Daltrop¶||, Edgar M. Harvat¶**, Lin Hong¶, Stuart J. Ferguson¶, and Teizo Kitagawa

From the Okazaki Institute for Integrative Bioscience, National Institutes of Natural Sciences, Myodaiji, Okazaki, Aichi 444-8787, Japan and the ^¶Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom

The heme chaperone CcmE is a novel protein that binds heme covalently via a histidine residue as part of its essential function in the process of cytochrome c biogenesis in many bacteria as well as plant mitochondria. In the continued absence of a structure of the holoform of CcmE, identification of the heme ligands is an important step in understanding the molecular function of this protein and the role of covalent heme binding to CcmE during the maturation of c-type cytochromes. In this work, we present spectroscopic data that provide insight into the ligation of the heme iron in the soluble domain of CcmE from Escherichia coli. Resonance Raman spectra demonstrated that one of the heme axial ligands is a histidine residue and that the other is likely to be Tyr¹³⁴. In addition, the properties of the heme resonances of the holo-protein as compared with those of a form of CcmE with non-covalently bound heme provide evidence for the modification of one of the heme vinyl side chains by the protein, most likely the 2-vinyl group.

Received for publication, August 5, 2004 , and in revised form, September 27, 2004.

^* This study was supported in part by Grant-in-aid for Scientific Research 14001004 from the Ministry of Culture, Education, Sports, Science, and Technology of Japan (to T. K.) and Grant C20071 from the Biotechnology and Biological Sciences Research Council (BBSRC) (to S. J. F.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

^|| A Junior Research Fellow of Christ Church, Oxford.

^** A recipient of an Erasmus Scholarship from the European Union.

To whom correspondence should be addressed. Tel: 81-564-59-5225; Fax: 81-564-59-5229; E-mail: teizo{at}ims.ac.jp.

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