Shewanella oneidensis MR-1 is a sediment organism capable of dissimilatory reduction of insoluble metal compounds such as those of Fe(II) and Mn(IV). This bacterium has been used as a model organism for potential applications in bioremediation of contaminated environments and in the production of energy in microbial fuel cells. The capacity of Shewanella to perform extracellular reduction of metals is linked to the action of several multihaem cytochromes that may be periplasmic or can be associated with the inner or outer membrane. One of these cytochromes is CymA, a membrane-bound tetrahaem cytochrome localized in the periplasm that mediates the electron transfer between the quinone pool in the cytoplasmic membrane and several periplasmic proteins. Although CymA has the capacity to regulate multiple anaerobic respiratory pathways, little is known about the structure and functional mechanisms of this focal protein. Understanding the structure and function of membrane proteins is hampered by inherent difficulties associated with their purification since the choice of the detergents play a critical role in the protein structure and stability. In the present mini-review, we detail the current state of the art in the characterization of CymA, and add recent information on haem structural behaviour for CymA solubilized in different detergents. These structural differences are deduced from NMR spectroscopy data that provide information on the geometry of the haem axial ligands. At least two different conformational forms of CymA are observed for different detergents, which seem to be related to the micelle size. These results provide guidance for the discovery of the most promising detergent that mimics the native lipid bilayer and is compatible with biochemical and structural studies.
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December 2012
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Conference Article|
November 21 2012
The quest to achieve the detailed structural and functional characterization of CymA
Ricardo O. Louro;
Ricardo O. Louro
1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República–Estação Agronómica Nacional, 2780-157 Oeiras, Portugal
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Catarina M. Paquete
Catarina M. Paquete
1
1Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República–Estação Agronómica Nacional, 2780-157 Oeiras, Portugal
1To whom correspondence should be addressed (emailcpaquete@itqb.unl.pt).
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Publisher: Portland Press Ltd
Received:
April 27 2012
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2012 The Authors Journal
2012
Biochem Soc Trans (2012) 40 (6): 1291–1294.
Article history
Received:
April 27 2012
Citation
Ricardo O. Louro, Catarina M. Paquete; The quest to achieve the detailed structural and functional characterization of CymA. Biochem Soc Trans 1 December 2012; 40 (6): 1291–1294. doi: https://doi.org/10.1042/BST20120114
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