{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,13]],"date-time":"2026-04-13T01:08:38Z","timestamp":1776042518365,"version":"3.50.1"},"reference-count":26,"publisher":"Portland Press Ltd.","issue":"6","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2012,12,1]]},"abstract":"<jats:p>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.<\/jats:p>","DOI":"10.1042\/bst20120114","type":"journal-article","created":{"date-parts":[[2012,11,23]],"date-time":"2012-11-23T17:09:55Z","timestamp":1353690595000},"page":"1291-1294","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":13,"title":["The quest to achieve the detailed structural and functional characterization of CymA"],"prefix":"10.1042","volume":"40","author":[{"given":"Ricardo\u00a0O.","family":"Louro","sequence":"first","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Av. da Rep\u00fablica\u2013Esta\u00e7\u00e3o Agron\u00f3mica Nacional, 2780-157 Oeiras, Portugal"}]},{"given":"Catarina\u00a0M.","family":"Paquete","sequence":"additional","affiliation":[{"name":"Instituto de Tecnologia Qu\u00edmica e Biol\u00f3gica, Universidade Nova de Lisboa, Av. da Rep\u00fablica\u2013Esta\u00e7\u00e3o Agron\u00f3mica Nacional, 2780-157 Oeiras, Portugal"}]}],"member":"288","published-online":{"date-parts":[[2012,11,21]]},"reference":[{"key":"2021111720433269300_B1","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1146\/annurev.mi.48.100194.001523","article-title":"Iron and manganese in anaerobic respiration: environmental significance, physiology, and regulation","volume":"48","author":"Nealson","year":"1994","journal-title":"Annu. Rev. Microb."},{"key":"2021111720433269300_B2","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1089\/15362310252780834","article-title":"Gene and protein expression profiles of Shewanella oneidensis during anaerobic growth with different electron acceptors","volume":"6","author":"Beliaev","year":"2002","journal-title":"OMICS"},{"key":"2021111720433269300_B3","doi-asserted-by":"crossref","first-page":"6232","DOI":"10.1128\/jb.172.11.6232-6238.1990","article-title":"Respiration-linked proton translocation coupled to anaerobic reduction of manganese(IV) and iron(III) in Shewanella putrefaciens MR-1","volume":"172","author":"Myers","year":"1990","journal-title":"J. Bacteriol."},{"key":"2021111720433269300_B4","doi-asserted-by":"crossref","first-page":"1118","DOI":"10.1038\/nbt749","article-title":"Genome sequence of the dissimilatory metal ion-reducing bacterium Shewanella oneidensis","volume":"20","author":"Heidelberg","year":"2002","journal-title":"Nat. Biotechnol."},{"key":"2021111720433269300_B5","first-page":"455","article-title":"Impacts of Shewanella oneidensis c-type cytochromes","volume":"3","author":"Gao","year":"2010","journal-title":"Appl. Microbiol."},{"key":"2021111720433269300_B6","doi-asserted-by":"crossref","first-page":"9491","DOI":"10.1021\/bi034456f","article-title":"The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis","volume":"42","author":"Schwalb","year":"2003","journal-title":"Biochemistry"},{"key":"2021111720433269300_B7","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1007\/s00203-007-0321-y","article-title":"The influence of cultivation methods on Shewanella oneidensis physiology and proteome expression","volume":"189","author":"Elias","year":"2008","journal-title":"Arch. Microb."},{"key":"2021111720433269300_B8","doi-asserted-by":"crossref","first-page":"2283","DOI":"10.1128\/JB.01698-06","article-title":"The cymA gene, encoding a tetraheme c-type cytochrome, is required for arsenate respiration in Shewanella species","volume":"189","author":"Murphy","year":"2007","journal-title":"J. Bacteriol."},{"key":"2021111720433269300_B9","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1128\/jb.179.4.1143-1152.1997","article-title":"Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1","volume":"179","author":"Myers","year":"1997","journal-title":"J. Bacteriol."},{"key":"2021111720433269300_B10","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1016\/j.jmb.2008.05.066","article-title":"Quinol oxidation by c-type cytochromes: structural characterization of the menaquinol binding site of NrfHA","volume":"381","author":"Rodrigues","year":"2008","journal-title":"J. Mol. Biol."},{"key":"2021111720433269300_B11","doi-asserted-by":"crossref","first-page":"8515","DOI":"10.1074\/jbc.275.12.8515","article-title":"Purification and magneto-optical spectroscopic characterization of cytoplasmic membrane and outer membrane multiheme c-type cytochromes from Shewanella frigidimarina NCIMB400","volume":"275","author":"Field","year":"2000","journal-title":"J. Biol. Chem."},{"key":"2021111720433269300_B12","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1042\/BJ20120197","article-title":"A functional description of CymA, an electron transfer hub supporting anaerobic respiratory flexibility in Shewanella","volume":"444","author":"Marritt","year":"2012","journal-title":"Biochem. J."},{"key":"2021111720433269300_B13","doi-asserted-by":"crossref","first-page":"797","DOI":"10.1007\/s00203-009-0511-x","article-title":"Lysine-91 of the tetraheme c-type cytochrome CymA is essential for quinone interaction and arsenate respiration in Shewanella sp","volume":"191","author":"Zargar","year":"2009","journal-title":"Arch. Microb."},{"key":"2021111720433269300_B14","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1042\/bst0300658","article-title":"The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella","volume":"30","author":"Schwalb","year":"2002","journal-title":"Biochem. Soc. Trans."},{"key":"2021111720433269300_B15","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1007\/s00775-010-0623-4","article-title":"A systematic investigation of multiheme c-type cytochromes in prokaryotes","volume":"15","author":"Sharma","year":"2010","journal-title":"J. Biol. Inorg. Chem."},{"key":"2021111720433269300_B16","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1111\/j.1432-1033.1995.tb20208.x","article-title":"Determination of haem electronic structure in His-Met cytochromes c by 13C-NMR: the effect of the axial ligands","volume":"227","author":"Turner","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"2021111720433269300_B17","doi-asserted-by":"crossref","first-page":"12713","DOI":"10.1039\/c1dt10975h","article-title":"Orientation of the axial ligands and magnetic properties of the hemes in the cytochrome c7 family from Geobacter sulfurreducens determined by paramagnetic NMR","volume":"40","author":"Dantas","year":"2011","journal-title":"Dalton Trans."},{"key":"2021111720433269300_B18","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1016\/S0014-5793(02)03610-4","article-title":"Determination of the orientation of the axial ligands and of the magnetic properties of the haems in the tetrahaem ferricytochrome from Shewanella frigidimarina","volume":"531","author":"Louro","year":"2002","journal-title":"FEBS Lett."},{"key":"2021111720433269300_B19","doi-asserted-by":"crossref","first-page":"13240","DOI":"10.1021\/ja983102m","article-title":"Electronic structure of low-spin ferric porphyrins: 13C NMR studies of the influence of axial ligand orientation","volume":"120","author":"Louro","year":"1998","journal-title":"J. Am. Chem. Soc."},{"key":"2021111720433269300_B20","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1007\/s00775-010-0643-0","article-title":"The effect of detergents and lipids on the properties of the outer-membrane protein OmcA from Shewanella oneidensis","volume":"15","author":"Bodemer","year":"2010","journal-title":"J. Biol. Inorg. Chem."},{"key":"2021111720433269300_B21","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1007\/s00775-008-0398-z","article-title":"Electrochemical interrogations of the Mtr cytochromes from Shewanella: opening a potential window","volume":"13","author":"Firer-Sherwood","year":"2008","journal-title":"J. Biol. Inorg. Chem."},{"key":"2021111720433269300_B22","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.bbabio.2008.11.007","article-title":"Tuning of functional heme reduction potentials in Shewanella fumarate reductases","volume":"1789","author":"Pessanha","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720433269300_B23","doi-asserted-by":"crossref","first-page":"10370","DOI":"10.1074\/jbc.M109.078337","article-title":"Molecular basis for directional electron transfer","volume":"285","author":"Paquete","year":"2010","journal-title":"J. Biol. Chem."},{"key":"2021111720433269300_B24","doi-asserted-by":"crossref","first-page":"4259","DOI":"10.1039\/B917952F","article-title":"Molecular details of multielectron transfer: the case of multiheme cytochromes from metal respiring organisms","volume":"39","author":"Paquete","year":"2010","journal-title":"Dalton Trans."},{"key":"2021111720433269300_B25","first-page":"128","article-title":"Efficient detection of paramagnetically shifted NMR resonances by optimizing the WEFT pulse sequence","volume":"51","author":"Inubushi","year":"1983","journal-title":"J. Magn. Res."},{"key":"2021111720433269300_B26","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1186\/1472-6807-7-74","article-title":"NMR spectroscopic and analytical ultracentrifuge analysis of membrane protein detergent complexes","volume":"7","author":"Maslennikov","year":"2007","journal-title":"BMC Struct. Biol."}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/40\/6\/1291\/487650\/bst0401291.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/40\/6\/1291\/487650\/bst0401291.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,18]],"date-time":"2021-11-18T01:07:31Z","timestamp":1637197651000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/40\/6\/1291\/66752\/The-quest-to-achieve-the-detailed-structural-and"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,11,21]]},"references-count":26,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2012,11,21]]},"published-print":{"date-parts":[[2012,12,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bst20120114","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,11,21]]}}}