Operando film-electrochemical EPR spectroscopy tracks radical intermediates in surface-immobilized catalysts

Maryam Seif-Eddine, Samuel J. Cobb, Yunfei Dang, Kaltum Abdiaziz, Mark A. Bajada, Erwin Reisner & Maxie M. Roessler, Nat. Chem., 2024, DOI: 10.1038/s41557-024-01450-y

Understanding the effects of targeted modifications on the 1:2 Choline And GEranate structure

Ana Dobre, Spyridon Koutsoukos, Frederik Philippi, Daniel Rauber, Christopher W. M. Kay, Oriele Palumbo, Maxie M. Roessler and Tom Welton*,  Phys. Chem. Chem. Phys., 2024, DOI: 10.1039/D3CP05271K

Using light scattering to assess how phospholipid-protein interactions affect complex I functionality in liposomes

Jana Eisermann, John Joseph Wright, James Wilton-Ely, Judy Hirst and Maxie Roessler, RSC chem. biol., 2023, DOI: 10.1039/D2CB00158F

Radical-SAM dependent nucleotide dehydratase (SAND), rectification of the names of an ancient iron-sulfur enzyme using NC-IUBMB recommendations

Yuxuan Ji, Li Wei, Anqi Da, Holger Stark, Peter-Leon Hagedoorn, Simone Ciofi-Baffoni, Sally A. Cowley, Ricardo O. Louro, Smilja Todorovic, Maria Andrea Mroginski, Yvain Nicolet, Maxie M. Roessler, Nick E. Le Brun, Mario Piccioli, William S. James, Wilfred R. Hagen and Kourosh H. Ebrahimi*, Front. Mol. Biosci. 2022, DOI: 10.3389/fmolb.2022.1032220

Bio-Electrocatalytic Conversion of Food Waste to Ethylene via Succinic Acid as the Central Intermediate

Christian M. Pichler, Subhajit Bhattacharjee, Erwin Lam, Lin Su, Alberto Collauto, Maxie M. Roessler, Samuel J. Cobb, Vivek M. Badiani, Motiar Rahaman, and Erwin Reisner*, ACS Catal. 2022, DOI: 10.1021/acscatal.2c02689

Following the evolution of paramagnetic species during catalysis: film-electrochemical EPR spectroscopy

Maryam Seif-Eddine, Kaltum Abdiaziz, Mark Bajada, Erwin Reisner, Maxie M.Roessler, Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2022, DOI: 10.1016/j.bbabio.2022.148742

Controlling and exploiting intrinsic unpaired electrons in metalloproteins.

Katherine H. Richardson, Maryam Seif-Eddine, Adam Sills, Maxie M. Roessler, Methods in Enzymology, 2022, DOI: 10.1016/bs.mie.2022.02.014

Functional basis of electron transport within photosynthetic complex I

Katherine H. Richardson, John J. Wright, Mantas Šimėnas, Jacqueline Thiemann, Ana M. Esteves, Gemma McGuire, William K. Myers, John J. L. Morton, Michael Hippler, Marc M. Nowaczyk, Guy T. Hanke & Maxie M. Roessler, Nature Communications, 2021, DOI: 10.1038/s41467-021-25527-1

 

Rotaxane CoII Complexes as Field‐Induced Single‐Ion Magnets

Martina Cirulli, Enrico Salvadori, Zhi‐Hui Zhang, Michael Dommett, Floriana Tuna, Heiko Bamberger, James EM Lewis, Amanpreet Kaur, Graham J Tizzard, Joris Van Slageren, Rachel Crespo‐Otero, Stephen M Goldup, Maxie M Roessler, Angewandte Chemie International Edition, 2021. DOI: 10.1002/anie.202103596

Functional group introduction and aromatic unit variation in a set of π‑conjugated macrocycles: revealing the central role of local and global aromaticity

Martina Rimmele, Wojciech Nogala, Maryam Seif-Eddine, Maxie Roessler, Martin Heeney, Felix Plasser, Florian Glöcklhofer, Organic Chemistry Frontiers, 2021. DOI: 10.1039/D1QO00901J

Functional basis of electron transport within photosynthetic complex I

Katherine Hannah Richardson, John J Wright, Mantas Simenas, Jacqueline Thiemann, Ana Maria Esteves, Gemma McGuire, William K Myers, John JL Morton, MIchael Hippler, Marc M Nowaczyk, Guy Hanke, Maxie M Roessler, Nature Communications, volume 12, Article number: 5387, 2021. DOI: 10.1038/s41467-021-25527-1

A conserved arginine residue is critical for stabilizing the N2 FeS cluster in mitochondrial complex I

Mikhail A Hameedi, Daniel N Grba, Katherine H Richardson, Andrwe JY Jones, Wei Song, Maxie M Roessler, John J Wright, Judy Hirst, Journal of Biological Chemistry, volume 296, 100474, 2021. DOI: 10.1016/j.jbc.2021.100474

Insights into metalloproteins and metallodrugs from electron paramagnetic resonance spectroscopy

Jana Eisermann, Maryam Seif-Eddine, Maxie M.Roessler, Current Opinion in Chemical Biology, Volume 61, 2021, Pages 114-122. DOI: 10.1016/j.cbpa.2020.11.005

CurOp2021

A sensitivity leap for X-band EPR using a probehead with a cryogenic preamplifier

Mantas Šimėnas, James O’Sullivan, Christoph W Zollitsch, Oscar Kennedy, Maryam Seif-Eddine, Irina Ritsch, Miriam Hülsmann, Mian Qi, Adelheid Godt, Maxie M Roessler, Gunnar Jeschke, John JL Morton, Journal of Magnetic Resonance, Volume 3222020, Article 106876. DOI: 10.1016/j.jmr.2020.106876

JMR2021

Using a chimeric respiratory chain and EPR spectroscopy to determine the origin of semiquinone species previously assigned to mitochondrial complex I

John J Wright, Justin G Fedor, Judy Hirst, Maxie M Roessler, 2020, BMC Biol 18, 54, 2020. DOI: 10.1186/s12915-020-00768-6

Structure of inhibitor-bound mammalian complex I

Hannah R Bridges, Justin G Fedor, James N Blaza, Andrea Di Luca, Alexander Jussupow, Owen D Jarman, John J Wright, Ahmed-Noor A Agip, Ana P Gamiz-Hernandez, Maxie M Roessler, Ville RI Kaila, Judy Hirst, 2020Nat Commun 11, 5261 (2020). DOI: 10.1038/s41467-020-18950-3

A Precious‐Metal‐Free Hybrid Electrolyzer for Alcohol Oxidation Coupled to CO2‐to‐Syngas Conversion

Mark A Bajada, Souvik Roy, Julien Warnan, Kaltum Abdiaziz, Andreas Wagner, Maxie M Roessler, Erwin Reisner, 2020Angewandte Chemie, Vol: 132, Pages: 15763-15771, ISSN: 0044-8249. DOI: 10.1002/anie.202002680

Manipulating the Optical Properties of Carbon Dots by Fine‐Tuning their Structural Features

Hui Luo, Nikolaos Papaioannou, Enrico Salvadori, Maxie M Roessler, Gereon Ploenes, Ernst RH van Eck, Liviu C Tanase, Jingyu Feng, Yiwei Sun, Yan Yang, Mohsen Danaie, Ana Belen Jorge, Andrei Sapelkin, James Durrant, Stoichko D Dimitrov, Maria‐Magdalena Titirici, 2019, ChemSusChem, 12 (19), 4432-4441. DOI: 10.1002/cssc.201901795

Defining optimal electron transfer partners for light-driven cytochrome P450 reactions

Silas Busck Mellor, Marcos Hamborg Vinde, Agnieszka Zygadlo Nielsen, Guy Thomas Hanke, Kaltum Abdiaziz, Maxie M Roessler, Meike Burow, Mohammed Saddik Motawia, Birger Lindberg Møller, Poul Erik Jensen, 2019, Metabolic engineering, 55, 33-43. DOI 10.1016/j.ymben.2019.05.003

Protein film electrochemical EPR spectroscopy as a technique to investigate redox reactions in biomolecules

K. Abdiaziz, E. Salvadori, K. P. Sokol, E. Reisner, M. M. Roessler, 2019Chem. Commun., 2019,55, 8840-8843, DOI: 10.1039/C9CC03212F
Protein film electrochemical EPR spectroscopy as a technique to investigate redox reactions in biomolecules

Rotaxane-Based Transition Metal Complexes: Effect of the Mechanical Bond on Structure and Electronic Properties

M. Cirulli, A. Kaur, J.E.M. Lewis, Z. Zhang, J.A. Kitchen, S.M. Goldup*, M.M. Roessler* (2018), J. Am. Chem. Soc., DOI: 10.1021/jacs.8b09715

Interlocked HETEROLEPTIC Complexes

X-ray structural, functional and computational studies of the O 2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe-4S] cluster

A. Volbeda, J.-M. Mouesca, C. Darnault, M.M. Roessler, A. Parkin, F. A. Armstrong, J. C. Fontecilla-Camps* (2018), Chemical Communications, 54, 7175-7178. DOI: 10.1039/C8CC02896F

X-ray structural, functional and computational studies of the O 2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe-4S] cluster

Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

S. Martínez-Lumbreras, E. M. Krysztofinska, A. Thapaliya, A. Spilotros, D. Matak-Vinkovic, E. Salvadori, P. Roboti, Y. Nyathi, J. H. Muench, M. M. Roessler, D.I. Svergun, S. High , R. L. Isaacson* (2018), BMC Biology, 16, 76. DOI: 10.1186/s12915-018-0542-3

Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control

Principles and Applications of EPR Spectroscopy in the chemical sciences

M. M. Roessler* and E. Salvadori* (2018), Chemical Society Reviews, 47 (8), 2534-2553. DOI: 10.1039/C6CS00565A

Principles and Applications of EPR Spectroscopy in the chemical sciences

Using EPR Hyperfine Spectroscopy to define the Proton-Coupled Electron Transfer Reaction at Fe-S cluster N2 in Respiratory Complex


Using EPR Hyperfine Spectroscopy to define the Proton-Coupled Electron Transfer Reaction at Fe-S cluster N2 in Respiratory Complex IN. le Breton, J. J. Wright, A.J.Y.J. Jones, E. Salvadori, H. R. Bridges, J. Hirst, M. M. Roessler* (2017), J. Am. Chem. Soc., 139 (45), 16319-16326. DOI: 10.1021/jacs.7b09261 selected as Spotlight Article

Re-tuning the Catalytic Bias and Overpotential of a [NiFe]-hydrogenase via a Single Amino Acid Exchange at the Electron Entry/exit site

H. Adamson, M. Robinson, J. J. Wright, L. A. Flanagan, J. Walton, D. Elton, D. J. Gavaghan, A. M. Bond, M.M. Roessler, A. Parkin (2017),  J. Am. Chem. Soc., 139 (31), pp 10677-1068. DOI: 10.1021/jacs.7b03611

Re-tuning the Catalytic Bias and Overpotential of a [NiFe]-hydrogenase via a Single Amino Acid Exchange at the Electron Entry/exit site

Guiding Principles of Hydrogenase Catalysis Instigated and Clarified by Protein Film Electrochemistry

F. A. Armstrong*, R. M. Evans, S. V. Hexter, B. J. Murphy, M. M. Roessler, P. Wulff (2016), Acc. Chem. Res. 49 (5), pp 884-892. DOI: 10.1021/acs.accounts.6b00027

Guiding Principles of Hydrogenase Catalysis Instigated and Clarified by Protein Film Electrochemistry

Small-volume potentiometric titrations: EPR investigations of Fe-S cluster N2 in mitochondrial complex I

J. J. Wright, E. Salvadori, H. R. Bridges, J. Hirst & M. M. Roessler* (2016),  J. Inorg. Biochem. 162, pp 201-206. DOI: 10.1016/j.jinorgbio.2016.04.025

Small-volume potentiometric titrations: EPR investigations of Fe-S cluster N2 in mitochondrial complex I

Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance

L. A. Flanagan, J. J. Wright, M. M. Roessler, J.W. Moir & A. Parkin (2016), Chem. Commun. 52, pp 9133-9136. DOI: 10.1039/C6CC00515B

Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance

Energy conversion, redox catalysis and generation of reactive oxygen species by complex I

J. Hirst* & M. M. Roessler* (2016), BBA Bioenergetics. 1857 (7), pp 872-883. DOI: 10.1016/j.bbabio.2015.12.009

Energy conversion, redox catalysis and generation of reactive oxygen species by complex I

Discovery of Dark pH-dependent H+ Migration in a [NiFe]-hydrogenase and Its Mechanistic Relevance: Mobilising the Hydrido Ligand of the Ni-C Intermediate

B.J. Murphy,R. Hidalgo, M.M. Roessler, R.M. Evans, P.A. Ash, W.K. Myers, K.A. Vincent, and F.A. Armstrong (2015), J. Am. Chem. Soc. 137 (26), pp 8484-8489. DOI: 10.1021/jacs.5b03182

'Discovery of Dark pH-dependent H+ Migration in a [NiFe]-hydrogenase and Its Mechanistic Relevance: Mobilising the Hydrido Ligand of the Ni-C Intermediate

Principles of Sustained Enzymatic Hydrogen Oxidation in the Presence of Oxygen – The Crucial Influence of High Potential Fe–S Clusters in the Electron Relay of [NiFe]-Hydrogenases

R.M. Evans, A. Parkin, M.M. Roessler, B.J. Murphy, H. Adamson, M.J. Lukey, F. Sargent, A. Volbeda, J.C. Fontecilla-Camps, and F.A. Armstrong (2013), J. Am. Chem. Soc. 135 (7), pp 2694–2707. DOI: 10.1021/ja311055d

Principles of Sustained Enzymatic Hydrogen Oxidation in the Presence of Oxygen – The Crucial Influence of High Potential Fe–S Clusters in the Electron Relay of [NiFe]-Hydrogenases

EPR Spectroscopic Studies of the Fe–S Clusters in the O2-Tolerant [NiFe]-Hydrogenase Hyd-1 from Escherichia coli and Characterization of the Unique [4Fe–3S] Cluster by HYSCORE

M.M. Roessler, R.M. Evans, R.A. Davies, J. Harmer, and F.A. Armstrong (2012), J. Am. Chem. Soc. 134(37), pp 15581–15594. DOI: 10.1021/ja307117y

EPR Spectroscopic Studies of the Fe–S Clusters in the O2-Tolerant

X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli

A. Volbeda, P. Amara, C. Darnault, J.-M. Mouesca, A. Parkin, M.M. Roessler, F.A. Armstrong, J. C Fontecilla-Camps (2012),  Proceedings of the National Academy of Sciences 109 (14), pp 5305–5310. DOI: 10.1073/pnas.1119806109

X-ray crystallographic and computational studies of the O2-tolerant

How Salmonella oxidises H2 under aerobic conditions

A. Parkin, L. Bowman, M.M. Roessler, R.A. Davies, T. Palmer, F.A. Armstrong, and F. Sargent (2012), FEBS letters 586 (5), 536-544. DOI: 10.1016/j.febslet.2011.07.044

How Salmonella oxidises H2 under aerobic conditions

Oxygen-Tolerant [NiFe]-Hydrogenases: The Individual and Collective Importance of Supernumerary Cysteines at the Proximal Fe-S Cluster

M.J. Lukey, M.M. Roessler, A. Parkin, R.M. Evans, R.A. Davies, O. Lenz, B. Friedrich, F. Sargent, and F.A. Armstrong (2011), J. Am. Chem. Soc. 133 (42), pp 16881–16892. DOI: 10.1021/ja205393w

Oxygen-Tolerant

Theoretical and experimental investigation of surface-confined two-center metalloproteins by large-amplitude Fourier transformed ac voltammetry

C.Y. Lee, G.P. Stevenson, A. Parkin, M.M. Roessler, R.E. Baker, K. Gillow, D.J. Gavaghan, F.A. Armstrong, and A.M. Bond (2011), Journal of Electroanalytical Chemistry 656 (1), 293-303. 

Theoretical and experimental investigation of surface-confined two-center metalloproteins by large-amplitude Fourier transformed ac voltammetry

Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron–electron resonance

M.M. Roessler, M.S. King, A.J. Robinson, F.A. Armstrong, J. Harmer, and J. Hirst (2010), Proceedings of the National Academy of Sciences 107 (5), 1930-1935. DOI: 10.1073/pnas.0908050107

Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron–electron resonance

How Escherichia coli is equipped to oxidize hydrogen under different redox conditions

M.J. Lukey, A. Parkin, M.M. Roessler, B.J. Murphy, J. Harmer, T. Palmer, F. Sargent, and F.A. Armstrong (2010), Journal of Biological Chemistry 285 (6), 3928-3938. DOI: 10.1074/jbc.M109.067751

How Escherichia coli is equipped to oxidize hydrogen under different redox conditions