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A Functional Description Of Cyma, An Electron-Transfer Hub Supporting Anaerobic Respiratory Flexibility In Shewanella, Sophie J. Marritt, Thomas G. Lowe, Jordan Bye, Duncan G. G. Mcmillan, Liang Shi, James K. Fredrickson, John M. Zachara, David J. Richardson, Myles R. Cheesman, Lars J. C. Jeuken, Julea N. Butt
A Functional Description Of Cyma, An Electron-Transfer Hub Supporting Anaerobic Respiratory Flexibility In Shewanella, Sophie J. Marritt, Thomas G. Lowe, Jordan Bye, Duncan G. G. Mcmillan, Liang Shi, James K. Fredrickson, John M. Zachara, David J. Richardson, Myles R. Cheesman, Lars J. C. Jeuken, Julea N. Butt
US Department of Energy Publications
CymA (tetrahaem cytochrome c) is a member of the NapC/NirT family of quinol dehydrogenases. Essential for the anaerobic respiratory flexibility of shewanellae, CymA transfers electrons from menaquinol to various dedicated systems for the reduction of terminal electron acceptors including fumarate and insoluble minerals of Fe(III). Spectroscopic characterization of CymA from Shewanella oneidensis strain MR-1 identifies three lowspin His/His co-ordinated c-haems and a single high-spin chaem with His/H2O co-ordination lying adjacent to the quinolbinding site. At pH 7, binding of the menaquinol analogue, 2-heptyl-4-hydroxyquinoline-N-oxide, does not alter the midpoint potentials of the high-spin (approximately −240 mV) …
Exploring The Biochemistry At The Extracellular Redox Frontier Of Bacterial Mineral Fe(Iii) Respiration, David J. Richardson, Marcus J. Edwards, Gaye F. White, Nanakow Baiden, Robert S. Hartshorne, James K. Fredrickson, Liang Shi, John M. Zachara, Andrew J. Gates, University Of East Anglia, Thomas Clarke
Exploring The Biochemistry At The Extracellular Redox Frontier Of Bacterial Mineral Fe(Iii) Respiration, David J. Richardson, Marcus J. Edwards, Gaye F. White, Nanakow Baiden, Robert S. Hartshorne, James K. Fredrickson, Liang Shi, John M. Zachara, Andrew J. Gates, University Of East Anglia, Thomas Clarke
US Department of Energy Publications
Many species of the bacterial Shewanella genus are notable for their ability to respire in anoxic environments utilizing insoluble minerals of Fe(III) and Mn(IV) as extracellular electron acceptors. In Shewanella oneidensis, the process is dependent on the decahaem electron-transport proteins that lie at the extracellular face of the outer membrane where they can contact the insoluble mineral substrates. These extracellular proteins are charged with electrons provided by an inter-membrane electron-transfer pathway that links the extracellular face of the outer membrane with the inner cytoplasmic membrane and thereby intracellular electron sources. In the present paper, we consider the common structural …