Full Text Journal Articles by
Author Marcus J Edwards

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Uncovering nature's electronics.

Thomas A Clarke, Marcus J Edwards,

Nat. Chem. Biol. (Nature chemical biology)
[2020, 16(10):1041-1042]

Cited: 0 times

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His/Met heme ligation in the PioA outer membrane cytochrome enabling light-driven extracellular electron transfer by Rhodopseudomonas palustris TIE-1.

Dao-Bo Li, Marcus J Edwards, Anthony W Blake, Simone E Newton-Payne, Samuel E H Piper, Leon P Jenner, Katarzyna P Sokol, Erwin Reisner, Jessica H Van Wonderen, Thomas A Clarke, Julea N Butt,

A growing number of bacterial species are known to move electrons across their cell envelopes. Naturally this occurs in support of energy conservation and carbon-fixation. For biotechnology it allows electron exchange between bacteria and electrodes in microbial fuel cells and during microbial electrosynthesis. In this context Rhodopseudomonas palustris TIE-1 is ... Read more >>

Nanotechnology (Nanotechnology)
[2020, 31(35):354002]

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The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire.

Marcus J Edwards, Gaye F White, Julea N Butt, David J Richardson, Thomas A Clarke,

A growing number of bacteria are recognized to conduct electrons across their cell envelope, and yet molecular details of the mechanisms supporting this process remain unknown. Here, we report the atomic structure of an outer membrane spanning protein complex, MtrAB, that is representative of a protein family known to transport ... Read more >>

Cell (Cell)
[2020, 181(3):665-673.e10]

Cited: 0 times

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Role of multiheme cytochromes involved in extracellular anaerobic respiration in bacteria.

Marcus J Edwards, David J Richardson, Catarina M Paquete, Thomas A Clarke,

Heme containing proteins are involved in a broad range of cellular functions, from oxygen sensing and transport to catalyzing oxidoreductive reactions. The two major types of cytochrome (b-type and c-type) only differ in their mechanism of heme attachment, but this has major implications for their cellular roles in both localization ... Read more >>

Protein Sci. (Protein science : a publication of the Protein Society)
[2020, 29(4):830-842]

Cited: 1 time

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Membrane-spanning electron transfer proteins from electrogenic bacteria: Production and investigation.

Colin W J Lockwood, Jessica H van Wonderen, Marcus J Edwards, Samuel E H Piper, Gaye F White, Simone Newton-Payne, David J Richardson, Thomas A Clarke, Julea N Butt,

Certain bacterial species have a natural ability to exchange electrons with extracellular redox partners. This behavior allows coupling of catalytic transformations inside bacteria to complementary redox transformations of catalysts and electrodes outside the cell. Electricity generation can be coupled to waste-water remediation. Industrially relevant oxidation reactions can proceed exclusively when ... Read more >>

Meth. Enzymol. (Methods in enzymology)
[2018, 613:257-275]

Cited: 0 times

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Characterization of MtoD from Sideroxydans lithotrophicus: a cytochrome c electron shuttle used in lithoautotrophic growth.

Christopher R Beckwith, Marcus J Edwards, Matthew Lawes, Liang Shi, Julea N Butt, David J Richardson, Thomas A Clarke,

The autotrophic Sideroxydans lithotrophicus ES-1 can grow by coupling the oxidation of ferrous iron to the reduction of oxygen. Soluble ferrous iron is oxidized at the surface of the cell by an MtoAB porin-cytochrome complex that functions as an electron conduit through the outer membrane. Electrons are then transported to ... Read more >>

(Frontiers in microbiology)
[2015, 6:332]

Cited: 7 times

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Redox Linked Flavin Sites in Extracellular Decaheme Proteins Involved in Microbe-Mineral Electron Transfer.

Marcus J Edwards, Gaye F White, Michael Norman, Alice Tome-Fernandez, Emma Ainsworth, Liang Shi, Jim K Fredrickson, John M Zachara, Julea N Butt, David J Richardson, Thomas A Clarke,

Extracellular microbe-mineral electron transfer is a major driving force for the oxidation of organic carbon in many subsurface environments. Extracellular multi-heme cytochromes of the Shewenella genus play a major role in this process but the mechanism of electron exchange at the interface between cytochrome and acceptor is widely debated. The ... Read more >>

Sci Rep (Scientific reports)
[2015, 5:11677]

Cited: 36 times

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A trans-outer membrane porin-cytochrome protein complex for extracellular electron transfer by Geobacter sulfurreducens PCA.

Yimo Liu, Zheming Wang, Juan Liu, Caleb Levar, Marcus J Edwards, Jerome T Babauta, David W Kennedy, Zhi Shi, Haluk Beyenal, Daniel R Bond, Thomas A Clarke, Julea N Butt, David J Richardson, Kevin M Rosso, John M Zachara, James K Fredrickson, Liang Shi,

The multi-heme, outer membrane c-type cytochrome (c-Cyt) OmcB of Geobacter sulfurreducens was previously proposed to mediate electron transfer across the outer membrane. However, the underlying mechanism has remained uncharacterized. In G. sulfurreducens, the omcB gene is part of two tandem four-gene clusters, each is predicted to encode a transcriptional factor (OrfR/OrfS), ... Read more >>

Environ Microbiol Rep (Environmental microbiology reports)
[2014, 6(6):776-785]

Cited: 45 times

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A new crystal structure of the bifunctional antibiotic simocyclinone D8 bound to DNA gyrase gives fresh insight into the mechanism of inhibition.

Stephen J Hearnshaw, Marcus J Edwards, Clare E Stevenson, David M Lawson, Anthony Maxwell,

Simocyclinone D8 (SD8) is an antibiotic produced by Streptomyces antibioticus that targets DNA gyrase. A previous structure of SD8 complexed with the N-terminal domain of the DNA gyrase A protein (GyrA) suggested that four SD8 molecules stabilized a tetramer of the protein; subsequent mass spectrometry experiments suggested that a protein ... Read more >>

J. Mol. Biol. (Journal of molecular biology)
[2014, 426(10):2023-2033]

Cited: 13 times

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The X-ray crystal structure of Shewanella oneidensis OmcA reveals new insight at the microbe-mineral interface.

Marcus J Edwards, Nanakow A Baiden, Alexander Johs, Stephen J Tomanicek, Liyuan Liang, Liang Shi, Jim K Fredrickson, John M Zachara, Andrew J Gates, Julea N Butt, David J Richardson, Thomas A Clarke,

The X-ray crystal structure of Shewanella oneidensis OmcA, an extracellular decaheme cytochrome involved in mineral reduction, was solved to a resolution of 2.7 Å. The four OmcA molecules in the asymmetric unit are arranged so the minimum distance between heme 5 on adjacent OmcA monomers is 9 Å, indicative of ... Read more >>

FEBS Lett. (FEBS letters)
[2014, 588(10):1886-1890]

Cited: 21 times

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Molecular structure and free energy landscape for electron transport in the decahaem cytochrome MtrF.

Marian Breuer, Piotr Zarzycki, Liang Shi, Thomas A Clarke, Marcus J Edwards, Julea N Butt, David J Richardson, James K Fredrickson, John M Zachara, Jochen Blumberger, Kevin M Rosso,

The free energy profile for electron flow through the bacterial decahaem cytochrome MtrF has been computed using thermodynamic integration and classical molecular dynamics. The extensive calculations on two versions of the structure help to validate the method and results, because differences in the profiles can be related to differences in ... Read more >>

Biochem. Soc. Trans. (Biochemical Society transactions)
[2012, 40(6):1198-1203]

Cited: 10 times

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Analysis of structural MtrC models based on homology with the crystal structure of MtrF.

Marcus J Edwards, James K Fredrickson, John M Zachara, David J Richardson, Thomas A Clarke,

The outer-membrane decahaem cytochrome MtrC is part of the transmembrane MtrCAB complex required for mineral respiration by Shewanella oneidensis. MtrC has significant sequence similarity to the paralogous decahaem cytochrome MtrF, which has been structurally solved through X-ray crystallography. This now allows for homology-based models of MtrC to be generated. The ... Read more >>

Biochem. Soc. Trans. (Biochemical Society transactions)
[2012, 40(6):1181-1185]

Cited: 10 times

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The crystal structure of the extracellular 11-heme cytochrome UndA reveals a conserved 10-heme motif and defined binding site for soluble iron chelates.

Marcus J Edwards, Andrea Hall, Liang Shi, James K Fredrickson, John M Zachara, Julea N Butt, David J Richardson, Thomas A Clarke,

Members of the genus Shewanella translocate deca- or undeca-heme cytochromes to the external cell surface thus enabling respiration using extracellular minerals and polynuclear Fe(III) chelates. The high resolution structure of the first undeca-heme outer membrane cytochrome, UndA, reveals a crossed heme chain with four potential electron ingress/egress sites arranged within ... Read more >>

Structure (Structure (London, England : 1993))
[2012, 20(7):1275-1284]

Cited: 27 times

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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, Jim Fredrickson, Liang Shi, John Zachara, Andrew J Gates, Julea N Butt, Thomas A Clarke,

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 ... Read more >>

Biochem. Soc. Trans. (Biochemical Society transactions)
[2012, 40(3):493-500]

Cited: 11 times

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The 'porin-cytochrome' model for microbe-to-mineral electron transfer.

David J Richardson, Julea N Butt, Jim K Fredrickson, John M Zachara, Liang Shi, Marcus J Edwards, Gaye White, Nanakow Baiden, Andrew J Gates, Sophie J Marritt, Thomas A Clarke,

Many species of bacteria can couple anaerobic growth to the respiratory reduction of insoluble minerals containing Fe(III) or Mn(III/IV). It has been suggested that in Shewanella species electrons cross the outer membrane to extracellular substrates via 'porin-cytochrome' electron transport modules. The molecular structure of an outer-membrane extracellular-facing deca-haem terminus for ... Read more >>

Mol Microbiol (Molecular microbiology)
[2012, 85(2):201-212]

Cited: 69 times

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Identification and Characterization of MtoA: A Decaheme c-Type Cytochrome of the Neutrophilic Fe(II)-Oxidizing Bacterium Sideroxydans lithotrophicus ES-1.

Juan Liu, Zheming Wang, Sara M Belchik, Marcus J Edwards, Chongxuan Liu, David W Kennedy, Eric D Merkley, Mary S Lipton, Julea N Butt, David J Richardson, John M Zachara, James K Fredrickson, Kevin M Rosso, Liang Shi,

The Gram-negative bacterium Sideroxydans lithotrophicus ES-1 (ES-1) grows on FeCO(3) or FeS at oxic-anoxic interfaces at circumneutral pH, and the ES-1-mediated Fe(II) oxidation occurs extracellularly. However, the molecular mechanisms underlying ES-1's ability to oxidize Fe(II) remain unknown. Survey of the ES-1 genome for candidate genes for microbial extracellular Fe(II) oxidation ... Read more >>

(Frontiers in microbiology)
[2012, 3:37]

Cited: 51 times

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Mass spectrometry reveals that the antibiotic simocyclinone D8 binds to DNA gyrase in a "bent-over" conformation: evidence of positive cooperativity in binding.

Marcus J Edwards, Mark A Williams, Anthony Maxwell, Adam R McKay,

DNA topoisomerases are enzymes that control DNA topology and are vital targets for antimicrobial and anticancer drugs. Here we present a mass spectrometry study of complexes formed between the A subunit of the topoisomerase DNA gyrase and the bifunctional inhibitor simocyclinone D8 (SD8), an antibiotic isolated from Streptomyces. These studies ... Read more >>

Biochemistry (Biochemistry)
[2011, 50(17):3432-3440]

Cited: 9 times

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Crystallization and preliminary X-ray analysis of a complex formed between the antibiotic simocyclinone D8 and the DNA breakage-reunion domain of Escherichia coli DNA gyrase.

Marcus J Edwards, Ruth H Flatman, Lesley A Mitchenall, Clare E M Stevenson, Anthony Maxwell, David M Lawson,

Crystals of a complex formed between the 59 kDa N-terminal fragment of the Escherichia coli DNA gyrase A subunit (also known as the breakage-reunion domain) and the antibiotic simocyclinone D8 were grown by vapour diffusion. The complex crystallized with I-centred orthorhombic symmetry and X-ray data were recorded to a resolution ... Read more >>

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. (Acta crystallographica. Section F, Structural biology and crystallization communications)
[2009, 65(Pt 8):846-848]

Cited: 2 times

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A crystal structure of the bifunctional antibiotic simocyclinone D8, bound to DNA gyrase.

Marcus J Edwards, Ruth H Flatman, Lesley A Mitchenall, Clare E M Stevenson, Tung B K Le, Thomas A Clarke, Adam R McKay, Hans-Peter Fiedler, Mark J Buttner, David M Lawson, Anthony Maxwell,

Simocyclinones are bifunctional antibiotics that inhibit bacterial DNA gyrase by preventing DNA binding to the enzyme. We report the crystal structure of the complex formed between the N-terminal domain of the Escherichia coli gyrase A subunit and simocyclinone D8, revealing two binding pockets that separately accommodate the aminocoumarin and polyketide ... Read more >>

Science (Science (New York, N.Y.))
[2009, 326(5958):1415-1418]

Cited: 45 times

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