J. Butt

发表

Immobilized DNA hairpins for assay of sequential breaking and joining of DNA backbones.

R. Bowater, Benjamin O S Scott, Manuel Lavesa-Curto, 2006, Analytical biochemistry.

Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I. Changes in [4Fe-4S] cluster reduction potential and reactivity.

P. Stephens, G. Jensen, F. Armstrong, 1991, The Journal of biological chemistry.

Voltammetry of Adsorbed Redox Enzymes: Mechanisms in The Potential Dimension

F. Armstrong, J. Butt, 2008 .

Concentrating membrane proteins using asymmetric traps and AC electric fields.

S. Evans, P. Olmsted, J. P. Bramble, 2011, Journal of the American Chemical Society.

Characterization of Anammox Hydrazine Dehydrogenase, a Key N2-producing Enzyme in the Global Nitrogen Cycle*

S. de Vries, T. Barends, J. Keltjens, 2016, The Journal of Biological Chemistry.

Direct electrochemistry of Megasphaera elsdenii iron hydrogenase. Definition of the enzyme's catalytic operating potential and quantitation of the catalytic behaviour over a continuous potential range.

W. Hagen, J. Butt, M. Filipiak, 1997, European journal of biochemistry.

Which Multi-Heme Protein Complex Transfers Electrons More Efficiently? Comparing MtrCAB from Shewanella with OmcS from Geobacter.

J. Blumberger, J. Butt, Xiuyun Jiang, 2020, The journal of physical chemistry letters.

Exploring Step‐by‐Step Assembly of Nanoparticle:Cytochrome Biohybrid Photoanodes

Katherine L. Orchard, E. Hwang, E. Reisner, 2017, ChemElectroChem.

Opportunities for mesoporous nanocrystalline SnO2 electrodes in kinetic and catalytic analyses of redox proteins.

Li Xiaoe, J. Durrant, J. Butt, 2009, Biochemical Society transactions.

Mechanisms of Bacterial Extracellular Electron Exchange.

D. Richardson, J. Butt, G. White, 2016, Advances in microbial physiology.

Towards compartmentalized photocatalysis: multihaem proteins as transmembrane molecular electron conduits.

K. Critchley, E. Hwang, E. Reisner, 2019, Faraday discussions.

Quantum dot interactions with and toxicity to Shewanella oneidensis MR-1

K. Critchley, J. Butt, L. Jeuken, 2019, Nanotechnology.

Using direct electrochemistry to probe rate limiting events during nitrate reductase turnover.

D. Richardson, J. Butt, L. J. Anderson, 2000, Faraday discussions.

Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases.

R. M. Martínez-Espinosa, D. Richardson, M. Bonete, 2007, FEMS microbiology letters.

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

D. R. Bond, D. Richardson, K. Rosso, 2014, Environmental microbiology reports.

Rapid electron exchange between surface-exposed bacterial cytochromes and Fe(III) minerals

D. Richardson, A. Dohnalkova, J. Fredrickson, 2013, Proceedings of the National Academy of Sciences.

Role of a conserved glutamine residue in tuning the catalytic activity of Escherichia coli cytochrome c nitrite reductase.

D. Richardson, A. Hemmings, J. Cole, 2008, Biochemistry.

Bespoke Biomolecular Wires for Transmembrane Electron Transfer: Spontaneous Assembly of a Functionalized Multiheme Electron Conduit

A. Martel, E. Reisner, J. Butt, 2021, Frontiers in Microbiology.

Magnetic circular dichroism of hemoproteins with in situ control of electrochemical potential: "MOTTLE".

J. Butt, M. Cheesman, Jessica H van Wonderen, 2006, Analytical biochemistry.

The roles of CymA in support of the respiratory flexibility of Shewanella oneidensis MR-1.

D. Richardson, D. G. McMillan, J. Fredrickson, 2012, Biochemical Society transactions.

Structure of a bacterial cell surface decaheme electron conduit

John M. Zachara, Matthew J. Marshall, Julea N. Butt, 2011, Proceedings of the National Academy of Sciences.

Comparative structure-potentio-spectroscopy of the Shewanella outer membrane multiheme cytochromes

D. Richardson, J. Butt, T. Clarke, 2017 .

Enzyme Film Electrochemistry

D. Richardson, J. Butt, S. Marritt, 2015 .

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

D. Richardson, A. Johs, L. Liang, 2014, FEBS letters.

Controlling electron transfer at the microbe–mineral interface

D. Richardson, J. Butt, T. Clarke, 2013, Proceedings of the National Academy of Sciences.

Development of a proteoliposome model to probe transmembrane electron-transfer reactions.

D. Richardson, A. Dohnalkova, J. Fredrickson, 2012, Biochemical Society transactions.

Exploring the biochemistry at the extracellular redox frontier of bacterial mineral Fe(III) respiration.

D. Richardson, J. Fredrickson, J. Zachara, 2012, Biochemical Society transactions.

A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella.

J. Bye, D. Richardson, D. G. McMillan, 2012, The Biochemical journal.

Physiological function and catalytic versatility of bacterial multihaem cytochromes c involved in nitrogen and sulfur cycling.

O. Einsle, J. Butt, J. Simon, 2011, Biochemical Society transactions.

Structure and spectroscopy of the periplasmic cytochrome c nitrite reductase from Escherichia coli.

D. Richardson, A. Hemmings, A. Thomson, 2002, Biochemistry.

Explorations of time and electrochemical potential: opportunities for fresh perspectives on signalling proteins.

J. Butt, 2014, Biochemical Society transactions.

Characterization of a flavocytochrome that is induced during the anaerobic respiration of Fe3+ by Shewanella frigidimarina NCIMB400.

P. Dobbin, A. Powell, D. Richardson, 1999, The Biochemical journal.

The Impact of Enzyme Orientation and Electrode Topology on the Catalytic Activity of Adsorbed Redox Enzymes.

D. G. McMillan, J. Butt, L. Jeuken, 2013, Electrochimica acta.

Light-Driven H2 Evolution and C═C or C═O Bond Hydrogenation by Shewanella oneidensis: A Versatile Strategy for Photocatalysis by Nonphotosynthetic Microorganisms

D. Richardson, K. Waldron, G. Gall, 2017 .

A novel fluorescent probe for NAD-consuming enzymes.

R. Bowater, J. Butt, G. Wagner, 2011, Chemical communications.

Carbon Dots as Versatile Photosensitizers for Solar-Driven Catalysis with Redox Enzymes.

E. Reisner, J. Butt, B. Reuillard, 2016, Journal of the American Chemical Society.

Structural modeling of an outer membrane electron conduit from a metal-reducing bacterium suggests electron transfer via periplasmic redox partners

A. Martel, D. Richardson, D. Scott, 2018, The Journal of Biological Chemistry.

Redox and Chemical Activities of the Hemes in the Sulfur Oxidation Pathway Enzyme SoxAX*

B. Berks, A. Hemmings, J. Butt, 2012, The Journal of Biological Chemistry.

Multiple forms of the catalytic centre, CuZ, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus.

B. Berks, T. Rasmussen, A. Thomson, 2002, The Biochemical journal.

Resolution of key roles for the distal pocket histidine in cytochrome C nitrite reductases.

D. Richardson, J. Butt, M. Cheesman, 2015, Journal of the American Chemical Society.

Molecular interactions between multihaem cytochromes: probing the protein-protein interactions between pentahaem cytochromes of a nitrite reductase complex.

D. Richardson, J. Butt, T. Clarke, 2011, Biochemical Society transactions.

Kinetic and thermodynamic resolution of the interactions between sulfite and the pentahaem cytochrome NrfA from Escherichia coli.

D. Richardson, A. Hemmings, J. Butt, 2010, The Biochemical journal.

Look on the positive side! The orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases.

R. M. Martínez-Espinosa, D. Richardson, M. Bonete, 2007, FEMS microbiology letters.

Comparison of the structural and kinetic properties of the cytochrome c nitrite reductases from Escherichia coli, Wolinella succinogenes, Sulfurospirillum deleyianum and Desulfovibrio desulfuricans.

D. Richardson, A. Hemmings, J. Cole, 2006, Biochemical Society transactions.

Cytochrome c nitrite reductase: from structural to physicochemical analysis.

D. Richardson, A. Hemmings, J. Cole, 2005, Biochemical Society transactions.

Tuning a Nitrate Reductase for Function

D. Richardson, J. Butt, E. Flores, 2004, Journal of Biological Chemistry.

Catalytic Protein Film Electrochemistry Provides a Direct Measure of the Tetrathionate/Thiosulfate Reduction Potential.

J. Butt, C. Dahl, J. Kurth, 2015, Journal of the American Chemical Society.

Azotobacter vinelandii ferredoxin I. Aspartate 15 facilitates proton transfer to the reduced [3Fe-4S] cluster.

P. Stephens, G. Jensen, F. Armstrong, 1993, The Journal of biological chemistry.

Voltammetric studies of redox-active centers in metalloproteins adsorbed on electrodes.

F. Armstrong, J. Butt, A. Sucheta, 1993, Methods in enzymology.

Formation and properties of a stable ‘high-potential’ copper-iron-sulphur cluster in a ferredoxin

F. Armstrong, A. Thomson, J. Breton, 1994, Nature Structural Biology.

Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insights into the Mechanism of Oxidative Catalysis

E. Reisner, Jason C. Crack, J. Butt, 2022, Journal of the American Chemical Society.

Evidence for reversible multiple redox transformations of [3Fe‐4S] clusters

F. Armstrong, A. Thomson, J. Butt, 1989 .

Probing a complex of cytochrome c and cardiolipin by magnetic circular dichroism spectroscopy: implications for the initial events in apoptosis.

Michael T. Wilson, J. Butt, M. Cheesman, 2011, Journal of the American Chemical Society.

Multilayered Lipid Membrane Stacks for Biocatalysis Using Membrane Enzymes

S. Frielingsdorf, O. Lenz, J. Butt, 2017 .

Novel Redox Chemistry of [3Fe−4S] Clusters: Electrochemical Characterization of the All-Fe(II) Form of the [3Fe−4S] Cluster Generated Reversibly in Various Proteins and Its Spectroscopic Investigation in Sulfolobus acidocaldarius Ferredoxin

F. Armstrong, A. Thomson, J. Breton, 1996 .

Binding of thallium(I) to a [3Fe-4S] cluster: evidence for rapid and reversible formation of [Tl3Fe-4S]2+ and [Tl3Fe-4S]1+ centers in a ferredoxin

F. Armstrong, A. Thomson, J. Breton, 1991 .

High Performance Reduction of H2O2 with an Electron Transport Decaheme Cytochrome on a Porous ITO Electrode

E. Reisner, J. Butt, B. Reuillard, 2017, Journal of the American Chemical Society.

Spectroscopic and voltammetric characterisation of the bacterioferritin-associated ferredoxin of Escherichia coli.

M. Quail, P. Jordan, A. Thomson, 1996, Biochemical and biophysical research communications.

A decahaem cytochrome as an electron conduit in protein-enzyme redox processes.

J. Fontecilla-Camps, T. Laftsoglou, E. Hwang, 2016, Chemical communications.

Base-modified NAD and AMP derivatives and their activity against bacterial DNA ligases.

R. Field, R. Bowater, J. Butt, 2015, Organic & biomolecular chemistry.

Protein voltammetry and spectroscopy: integrating approaches

B. Berks, L. Male, J. Butt, 2008 .

Contrasting catalytic profiles of multiheme nitrite reductases containing CxxCK heme-binding motifs

V. Popov, J. Butt, J. Gwyer, 2013, JBIC Journal of Biological Inorganic Chemistry.

Identification of the iron-sulfur clusters in a ferredoxin from the archaeon Sulfolobus acidocaldarius. Evidence for a reduced [3Fe-4S] cluster with pH-dependent electronic properties.

F. Armstrong, Y. Pétillot, A. Thomson, 1995, European journal of biochemistry.

Investigation of metal ion uptake reactivities of [3Fe-4S] clusters in proteins : voltammetry of co-adsorbed ferredoxin-aminocyclitol films at graphite electrodes and spectroscopic identification of transformed clusters

F. Armstrong, A. Thomson, J. Breton, 1991 .

Avoided Level Crossing Muon Spectroscopy of Free Radicals Formed by Muonium Addition to the Constituents of DNA

P. Hubbard, J. Butt, V. Oganesyan, 2004 .

Redox-triggered events in cytochrome c nitrite reductase.

D. Richardson, J. Butt, J. Gwyer, 2004, Bioelectrochemistry.

Electrochemical titrations and reaction time courses monitored in situ by magnetic circular dichroism spectroscopy.

J. Butt, M. Cheesman, J. Bradley, 2011, Analytical biochemistry.

Spectropotentiometric and Structural Analysis of the Periplasmic Nitrate Reductase from Escherichia coli*

D. Richardson, A. Hemmings, J. Cole, 2007, Journal of Biological Chemistry.

Reductive activation of nitrate reductases.

D. Richardson, J. Butt, S. George, 2005, Dalton transactions.

The relationship between redox enzyme activity and electrochemical potential-cellular and mechanistic implications from protein film electrochemistry.

D. Richardson, A. Mayes, J. Butt, 2011, Physical chemistry chemical physics : PCCP.

Voltammetric characterization of the aerobic energy-dissipating nitrate reductase of Paracoccus pantotrophus: exploring the activity of a redox-balancing enzyme as a function of electrochemical potential.

D. Richardson, J. Butt, Andrew J. Gates, 2008, The Biochemical journal.

Inhibiting Escherichia coli cytochrome c nitrite reductase: voltammetry reveals an enzyme equipped for action despite the chemical challenges it may face in vivo.

D. Richardson, J. Butt, J. Gwyer, 2006, Biochemical Society transactions.

Electrocatalytic reduction of nitrate and selenate by NapAB.

D. Richardson, J. Butt, C. Butler, 2011, Biochemical Society transactions.

Catalytic protein film voltammetry from a respiratory nitrate reductase provides evidence for complex electrochemical modulation of enzyme activity.

D. Richardson, J. Butt, L. J. Anderson, 2001, Biochemistry.

Electrochemical Potential and pH Dependences of [3Fe-4S] ↔ [M3Fe-4S] Cluster Transformations (M = Fe, Zn, Co, and Cd) in Ferredoxin III from Desulfovibrio africanus and Detection of a Cluster with M = Pb

F. Armstrong, A. Thomson, J. Breton, 1997 .

Redox-active ferrocene-modified Cowpea mosaic virus nanoparticles.

G. Lomonossoff, A. Aljabali, J. E. Barclay, 2010, Dalton transactions.

Laying the foundation for understanding muon implantation in DNA: ab initio DFT calculations of the nucleic acid base muonium adducts

P. Hubbard, J. Butt, V. Oganesyan, 2003 .

The flavodoxin FldA activates the class Ia ribonucleotide reductase of Campylobacter jejuni

J. Butt, D. Kelly, Abdulmajeed G. Alqurashi, 2021, Molecular microbiology.

Layer-by-Layer Assembly of Supported Lipid Bilayer Poly-L-Lysine Multilayers.

G. Gilardi, J. Richens, P. O'shea, 2016, Biomacromolecules.

Menaquinone-7 Is Specific Cofactor in Tetraheme Quinol Dehydrogenase CymA

D. G. McMillan, J. Butt, L. Jeuken, 2012, The Journal of Biological Chemistry.

Multi-haem cytochromes in Shewanella oneidensis MR-1: structures, functions and opportunities

Jochen Blumberger, Marian Breuer, Kevin M Rosso, 2015, Journal of The Royal Society Interface.

Nanosecond heme-to-heme electron transfer rates in a multiheme cytochrome nanowire reported by a spectrally unique His/Met-ligated heme

I. Sazanovich, M. Towrie, S. Meech, 2021, Proceedings of the National Academy of Sciences.

Photosensitised Multiheme Cytochromes as Light‐Driven Molecular Wires and Resistors

Christopher R. Hall, J. Butt, Jessica H van Wonderen, 2018, Chembiochem : a European journal of chemical biology.

Protein–Protein Interaction Regulates the Direction of Catalysis and Electron Transfer in a Redox Enzyme Complex

S. Evans, S. Elliott, D. Richardson, 2013, Journal of the American Chemical Society.

Methylene blue as an electrochemical discriminator of single- and double-stranded oligonucleotides immobilised on gold substrates.

A J Thomson, A. Thomson, J. Butt, 2001, The Analyst.

The Nitric Oxide Reductase Activity of Cytochrome c Nitrite Reductase from Escherichia coli*

D. Richardson, J. Butt, M. Cheesman, 2008, Journal of Biological Chemistry.

Escherichia coli cytochrome c nitrite reductase NrfA.

D. Richardson, A. Hemmings, J. Hinton, 2008, Methods in enzymology.

The ‘porin–cytochrome’ model for microbe‐to‐mineral electron transfer

Liang Shi, D. Richardson, J. Fredrickson, 2012, Molecular microbiology.

Characterization of an electron conduit between bacteria and the extracellular environment

Paul C Mills, Liang Shi, Ming Tien, 2009, Proceedings of the National Academy of Sciences.

The hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant.

Michael T. Wilson, Lewis A Fraser, J. Worrall, 2013, The Biochemical journal.

Voltammetric study of proton-gated electron transfer in a mutant ferredoxin. Altering aspartate to asparagine blocks oxidation of the [3Fe-4S] cluster of Azotobacter vinelandii ferredoxin I

F. Armstrong, J. Butt, B. Burgess, 1993 .

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

Julea N. Butt, Liang Shi, Marcus J. Edwards, 2015, Front. Microbiol..

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

E. Reisner, J. Butt, Katarzyna P. Sokol, 2020, Nanotechnology.

Structural Basis of Biological NO Generation by Octaheme Oxidoreductases*

T. Barends, J. Keltjens, M. Jetten, 2013, The Journal of Biological Chemistry.

Photoreduction of Shewanella oneidensis Extracellular Cytochromes by Organic Chromophores and Dye‐Sensitized TiO2

D. Richardson, E. Hwang, E. Reisner, 2016, Chembiochem : a European journal of chemical biology.

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

M. Lipton, D. Richardson, E. Merkley, 2012, Front. Microbio..

Enzyme-catalysed nitrate reduction-themes and variations as revealed by protein film voltammetry.

D. Richardson, J. Butt, E. Flores, 2002, Bioelectrochemistry.

Different responses to muon implantation in single- and double-stranded DNA

P. Hubbard, J. Butt, V. Oganesyan, 2006 .

Making Connections: An Amphiphilic Ferrocene Stimulates Bacterial Electricity Production

J. Butt, T. Clarke, Jonathan A. Davies, 2017 .

Iron-sulphur clusters with labile metal ions.

F. Armstrong, A. Thomson, J. Breton, 1992, Journal of inorganic biochemistry.

Iron-sulphur clusters in electron transfer, catalysis and control.

F. Armstrong, A. Thomson, J. Breton, 1991, Biochemical Society transactions.

Biological approaches to artificial photosynthesis: general discussion.

Moritz F. Kuehnel, Han Sen Soo, M. Grätzel, 2019, Faraday discussions.

Electrochemistry of surface-confined enzymes: Inspiration, insight and opportunity for sustainable biotechnology

Leon P. Jenner, Julea N. Butt, J. Butt, 2018 .

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

D. Richardson, J. Fredrickson, J. Zachara, 2015, Scientific Reports.

Spectopotentiometric properties and salt-dependent thermotolerance of a [2Fe-2S] ferredoxin-involved nitrate assimilation in Haloferax mediterranei.

R. M. Martínez-Espinosa, D. Richardson, M. Bonete, 2007, FEMS microbiology letters.

The Crystal Structure of a Biological Insulated Transmembrane Molecular Wire

D. Richardson, J. Butt, G. White, 2020, Cell.

Characterization of Shewanella oneidensis MtrC: a cell-surface decaheme cytochrome involved in respiratory electron transport to extracellular electron acceptors

D. Richardson, J. Fredrickson, J. Zachara, 2007, JBIC Journal of Biological Inorganic Chemistry.

Voltammetry and in situ scanning tunneling microscopy of cytochrome C nitrite reductase on Au(111) electrodes.

J. Ulstrup, J. Butt, Jingdong Zhang, 2006, Biophysical journal.

Fresh Approaches and New Surprises with Iron-Sulfur Clusters

F. Armstrong, A. Thomson, J. Breton, 1992 .

A Decaheme Cytochrome as a Molecular Electron Conduit in Dye-Sensitized Photoanodes

Katherine L. Orchard, E. Hwang, Chong‐Yong Lee, 2015, Advanced functional materials.

Voltammetric characterization of rapid and reversible binding of an exogenous thiolate ligand at a [4Fe-4S] cluster in ferredoxin III from Desulfovibrio africanus

F. Armstrong, A. Thomson, J. Breton, 1993 .

Coherent Electron Transport across a 3 nm Bioelectronic Junction Made of Multi-Heme Proteins

M. Sheves, D. Cahen, Z. Futera, 2020, The journal of physical chemistry letters.

Off-resonant coherent electron transport over three nanometers in multi-heme protein bioelectronic junctions

M. Sheves, D. Cahen, Z. Futera, 2020, 2007.10384.

Direct evidence for heme-assisted solid-state electronic conduction in multi-heme c-type cytochromes† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc01716f

M. Sheves, D. Cahen, J. Blumberger, 2018, Chemical science.

Ultra-Fast Light-Driven Electron Transfer in a Ru(II)tris(bipyridine)-Labelled Multiheme Cytochrome.

I. Sazanovich, M. Towrie, S. Meech, 2019, Journal of the American Chemical Society.

Ultrafast Light-Driven Electron Transfer in a Ru(II)tris(bipyridine)-Labeled Multiheme Cytochrome

I. Sazanovich, M. Towrie, S. Meech, 2019 .

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

Piotr Zarzycki, Liang Shi, Jochen Blumberger, 2012, Biochemical Society transactions.

Heme ligation and redox chemistry in two bacterial thiosulfate dehydrogenase (TsdA) enzymes

E. Reisner, J. Butt, C. Dahl, 2019, The Journal of Biological Chemistry.

Electron Accepting Units of the Diheme Cytochrome c TsdA, a Bifunctional Thiosulfate Dehydrogenase/Tetrathionate Reductase*♦

M. Archer, J. Butt, I. Pereira, 2016, The Journal of Biological Chemistry.

Respiratory nitrate and nitrite pathway in the denitrifier haloarchaeon Haloferax mediterranei.

R. M. Martínez-Espinosa, D. Richardson, M. Bonete, 2006, Biochemical Society Transactions.

The 11‐Heme Cell‐Surface Cytochrome UndA of Shewanella sp. HRCR‐6

D. Richardson, J. Butt, Liang Shi, 2014 .

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

D. Richardson, J. Fredrickson, J. Zachara, 2012, Structure.

Diode or tunnel-diode characteristics? Resolving the catalytic consequences of proton coupled electron transfer in a multi-centered oxidoreductase.

D. Richardson, J. Butt, J. Gwyer, 2005, Journal of the American Chemical Society.

Influence of haem environment on the catalytic properties of the tetrathionate reductase TsdA from Campylobacter jejuni

J. Butt, C. Dahl, D. Kelly, 2016, Bioscience reports.

Spectroelectrochemical characterization of a pentaheme cytochrome in solution and as electrocatalytically active films on nanocrystalline metal-oxide electrodes.

Li Xiaoe, J. Durrant, J. Butt, 2008, Journal of the American Chemical Society.

Freely diffusing versus adsorbed protein: Which better mimics the cellular state of a redox protein?

D. Richardson, J. Butt, T. Clarke, 2013 .

Electrode assemblies composed of redox cascades from microbial respiratory electron transfer chains.

D. Richardson, D. G. McMillan, J. Butt, 2013, Biochemical Society transactions.

Resolving the contributions of the membrane-bound and periplasmic nitrate reductase systems to nitric oxide and nitrous oxide production in Salmonella enterica serovar Typhimurium.

D. Richardson, E. Baggs, J. Butt, 2012, The Biochemical journal.

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

D. Richardson, J. Butt, G. White, 2018, Methods in enzymology.

Electron transfer to the active site of the bacterial nitric oxide reductase is controlled by ligand binding to heme b₃.

D. Richardson, J. Butt, M. Roldán, 2011, Biochimica et Biophysica Acta.

Voltammetry of a flavocytochrome c(3): the lowest potential heme modulates fumarate reduction rates.

P. Dobbin, D. Richardson, J. Butt, 2000, Biophysical journal.

Tuning a Nitrate Reductase for Function THE FIRST SPECTROPOTENTIOMETRIC CHARACTERIZATION OF A BACTERIAL ASSIMILATORY NITRATE REDUCTASE REVEALS NOVEL REDOX PROPERTIES*

D. Richardson, J. Butt, E. Flores, 2004 .

A haloarchaeal ferredoxin electron donor that plays an essential role in nitrate assimilation.

R. M. Martínez-Espinosa, D. Richardson, M. Bonete, 2011, Biochemical Society transactions.

Differences in the RNA binding sites of iron regulatory proteins and potential target diversity.

R D Klausner, K Iwai, Seth M. Cohen, 1996, Proceedings of the National Academy of Sciences of the United States of America.

Characterization of the active site and calcium binding in cytochrome c nitrite reductases.

D. Richardson, A. Hemmings, J. Butt, 2011, Biochemical Society transactions.

Characterization of Anammox Hydrazine Dehydrogenase, a Key N2-producing Enzyme in the Global Nitrogen Cycle*

S. de Vries, T. Barends, J. Keltjens, 2016, The Journal of Biological Chemistry.

Rational Design of Covalent Multiheme Cytochrome‐Carbon Dot Biohybrids for Photoinduced Electron Transfer

E. Reisner, J. Butt, L. Jeuken, 2023, Advanced Functional Materials.

A functional description of CymA, an electron-transfer hub supporting anaerobic respiratory flexibility in Shewanella.

D. Richardson, D. G. McMillan, J. Fredrickson, 2012, The Biochemical journal.

Characterization of an electron conduit between bacteria and the extracellular environment

M. Tien, D. Richardson, J. Fredrickson, 2009, Proceedings of the National Academy of Sciences.

A haloarchaeal ferredoxin electron donor that plays an essential role in nitrate assimilation.

R. M. Martínez-Espinosa, D. Richardson, M. Bonete, 2011, Biochemical Society transactions.

Protein Film Voltammetry Reveals Distinctive Fingerprints of Nitrite and Hydroxylamine Reduction by a Cytochrome c Nitrite Reductase*

D. Richardson, J. Cole, J. Butt, 2002, The Journal of Biological Chemistry.

The Structure of a Biological Insulated Transmembrane Molecular Wire

D. Richardson, J. Butt, G. White, 2019, SSRN Electronic Journal.

Engineering of bespoke photosensitiser–microbe interfaces for enhanced semi-artificial photosynthesis

J. Butt, L. Jeuken, Erwin Reisner, 2024, Chemical science.

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

D. Richardson, J. Fredrickson, J. Zachara, 2012, Structure.

Concentrating membrane proteins using asymmetric traps and AC electric fields.

S. Evans, P. Olmsted, J. P. Bramble, 2011, Journal of the American Chemical Society.

Genetic Code Expansion in Shewanella oneidensis MR-1 Allows Site-Specific Incorporation of Bioorthogonal Functional Groups into a c-Type Cytochrome.

J. Butt, M. Edwards, Colin W. J. Lockwood, 2024, ACS synthetic biology.

Do multiheme cytochromes containing close-packed heme groups have a band structure formed from the heme π and π* orbitals?

J. Butt, Jessica H. van Wonderen, Jochen Blumberger, 2024, Current Opinion in Electrochemistry.

Spectral Properties of Bacterial Nitric-oxide Reductase

D. Richardson, A. Thomson, J. Butt, 2002, The Journal of Biological Chemistry.