NDLI: Metal and redox selectivity of protoporphyrin binding to the heme chaperone CcmE

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Metallomics Vol - 3 Issue - 3

Metallomics Vol - 3 Issue - 2

Metallomics Vol -2

Metallomics Vol -1

Metal and redox selectivity of protoporphyrin binding to the heme chaperone CcmE

Content Provider	Royal Society of Chemistry (RSC)
Author	Moreau, Matthew Harvat, Edgar M. Sobott, Frank Ferguson, Stuart J. Stevens, Julie M. Daltrop, Oliver Barker, Paul D.
Copyright Year	2011
Abstract	The interaction of heme with the heme chaperone CcmE is central to our understanding of cytochrome c maturation, a complex post-translational process involving at least eight proteins in many Gram-negative bacteria and plant mitochondria. We have shown previously that Escherichia coli CcmE can interact with heme non-covalently in vitro, before forming a novel covalent histidine-heme bond, in a redox-sensitive manner. The function of CcmE is to bind heme in the periplasm before transferring it to apocytochromes c. In the absence of structural information on the complex of CcmE and heme, we have further characterized it by examining the binding of the soluble domain of CcmE (CcmE′) to protoporphyrins containing metals other than Fe, namely Zn-, Sn-, Co- and Mn-protoporphyrin (PPIX). CcmE′ demonstrated no affinity for the Zn- or Sn-containing protoporphyrins and low affinity for Mn(II)-PPIX. High-affinity, reversible binding was, however, observed for Co(III)-PPIX, which was highly sensitive to oxidation state as demonstrated by release of the ligand from the chaperone on reduction; no binding to Co(II)-PPIX was observed. The non-covalent complex of CcmE′ and Co(III)-PPIX was characterized by non-denaturing mass spectrometry. The implications of these observations for the in vivo function of CcmE are discussed.
Starting Page	363
Ending Page	368
Page Count	6
File Format	HTM / HTML PDF
ISSN	17565901
Volume Number	3
Issue Number	4
Journal	Metallomics
DOI	10.1039/c0mt00085j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Mitochondrion Escherichia Co-chaperone Ligand Escherichia coli Interaction Covalent bond Periplasm Gram-negative bacteria Protoporphyrin IX Mass spectrometry
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Metals and Alloys Biochemistry Biomaterials Biophysics

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