Book chapters

  1. Kappler U. and Maher M. J., ‘SoxAX Cytochromes’ (2013) in Encyclopedia of Inorganic and Bioinorganic Chemistry, Albrecht Messerschmidt Ed, Wiley, New Jersey, published online 23.09.2013.
  2. Lee M., Maher M. J., Christopherson R. I. and Guss J. M. ‘Dihydroorotase Inhibitors’ (2009) in Drug Design of Zinc-Enzyme Inhibitors, Claudiu T. Supuran and Jean-Yves Winum Eds, Wiley, New Jersey, 981-988.

Refereed Journal articles 

  1. Maghool S., Cooray D. N. G., Stroud D. A., Aragão D., Ryan M. T., Maher M. J. ‘Structural and functional characterization of the mitochondrial complex IV assembly factor Coa6.’ (2019) Life science alliance, 2,
  2. Casas Garcia G. P., Perugini M. A., Lamont I. L., Maher M. J., ‘The purification of the σFpvI/FpvR20 and σPvdS/FpvR20 protein complexes is facilitated at room temperature.’ (2019) Protein Express. Purific., 160, 11-18.
  3. Monk I. R., Shaikh N., Begg S. L., Gajdiss M., Sharkey L. K. R, Lee J. Y. H., Pidot S. J., Seemann T., Kuiper M., Winnen B., Hvorup R., Collins B. M., Bierbaum G., Udagedara S. R., Morey J. R., Pulyani N., Howden B. P., Maher M. J., McDevitt C. A., King G. F., Stinear T. P. ‘Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus.’ (2019) Nat. Comm. 10, 1-13.
  4. Maghool S., La Fontaine S., Maher M. J., ‘High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.’ (2019) Acta Crystallogr F Struct Biol Commun. 75, 392-396.
  5. Udagedara S. R., Wijekoon C. J. K., Xiao Z., Wedd A. G., Maher M. J. (2019) ‘The crystal structure of the CopC protein from Pseudomonas fluorescens reveals amended classifications for the CopC protein family.’ (2019) J Inorg Biochem., 195,194-200.
  6. Sikanyika M., Aragão D., McDevitt C. A., Maher M. J. ‘The structure and activity of the glutathione reductase from Streptococcus pneumoniae.’ (2019) Acta Crystallogr F Struct Biol Commun. 75, 54-61.
  7. Maher M.J., Herath A.S., Udagedara S.R., Dougan D.A. and Truscott K.N. ‘Crystal structure of bacterial succinate:quinone oxidoreductase flavoprotein SdhA in complex with its assembly factor SdhE’ (2018) Natl. Acad. Sci. USA, 115, 2982-2987. # joint corresponding author
  8. Lee M., Cooray N.D.G.,Maher M.J. ‘The crystal structures of a copper-bound metallochaperone from Saccharomyces cerevisiae.’ (2017) J Inorg Biochem., 177, 368-374.
  9. Edgar R.J., Hampton G.E., Garcia G.P.C.,Maher M.J., Perugini M.A., Ackerley D.F., Lamont I.L. ‘Integrated activities of two alternative sigma factors coordinate iron acquisition and uptake by Pseudomonas aeruginosa.’ (2017) Mol Microbiol. 106, 891-904.
  10. Hsiao J.C., McGrath A.P., Kielmann L., Kalimuthu P., Darain F., Bernhardt P.V., Harmer J., Lee M., Meyers K.,Maher M.J.#, Kappler U#. ‘The central active site arginine in sulfite oxidizing enzymes alters kinetic properties by controlling electron transfer and redox interactions.’ (2017) Biochim Biophys Acta., 18591, 19-27. # joint corresponding author
  11. McGrath P., Laming E. M., Guss J. M., Trewhella J., Calmes B., Bernhardt P. V., Hanson G. R., Kappler U, Maher M. J. ‘Structural basis of interprotein electron transfer in bacterial sulfite oxidation’ (2015) eLife, 10.7554/eLife.09066.
  12. Stroud D. A., Maher M. J., Lindau C., Vögtle F. N., Frazier A. E., Surgenor E., Mountford H., Singh A. P., Bonas M., Oeljeklaus S., Warscheid B., Meisinger C., Thorburn D. R., Ryan M. T. ‘COA6 is a mitochondrial IV assembly factor critical for biogenesis of mtDNA-encoded COX2.’ (2015) Hum. Mol. Genet., 24, 5404-15.
  13. *Begg S. L., Eijkelkamp B. A., Luo Z., Couñago R. M., Morey J. R., Maher M. J., Kobe B., O’Mara M. L., Paton J. C., McDevitt C. A. ‘Dysregulation of transition metal-ion homeostasis is the molecular basis for cadmium toxicity in Streptococcus pneumoniae.’ (2015) Nat. Commun., 6:6418.
  14. Guilfoyle A. P., Deshpande C. N., Font J. Ash M. R., Tourle S., Schenk G., Maher M. J.#, Jormakka M.# ‘A GTPase Chimera Illustrates an Uncoupled Nucleotide Affinity and Release Rate, Providing Insight into the Activation Mechanism.’ (2014) Biophys. J., 107, L45-8. #joint corresponding author
  15. Guilfoyle A. P., Deshpande C. N., Schenk G., Maher M. J., Jormakka M. ‘Exploring the correlation between the sequence composition of the nucleotide binding G5 loop of the FeoB GTPase domain (NFeoB) and the intrinsic GDP release rate’ (2014) Biosci. Rep., 34, e00158.
  16. Guilfoyle A. P., Deshpande C. N., Vincent K., Pedroso M. M., Schenk G., Maher M. J., Jormakka M. ‘Structural and functional analysis of a FeoB A143S G5 loop mutant explains the accelerated GDP release rate’ (2014) FEBS J., 281, 2254-65.
  17. Kappler U. and Maher M. J. ‘The bacterial SoxAX cytochromes’ (2013) Cell Mol. Life. Sci., 70, 977-92.
  18. Deshpande C. N., McGrath A. P., Font J., Guilfoyle A. P., Maher M. J., Jormaka M. ‘Structure of an atypical FeoB G-domain reveals a putative domain-swapped dimer’ (2013) Acta Cryst., F69, 399-404.
  19. Iwata M., Lee Y., Yamashita T., Yagi T., Iwata S., Cameron A. D. Maher M. J. ‘The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates’ (2012) Proc. Natl. Acad. Sci. USA, 109, 15247-52.
  20. Laming E. M., McGrath A. P. Guss J. M., Kappler U. and Maher M. J. ‘The X-ray crystal structure of a pseudoazurin from Sinorhizobium meliloti’ (2012) J. Inorg. Biochem., 115, 148-54.
  21. Ash M. R., Maher M. J., Guss J. M. and Jormakka M. ‘The cation-dependent G-proteins: in a class of their own’ (2012) FEBS Lett., 586, 2218-24.
  22. Ash M.-R., Maher M. J., Guss J. M. and Jormakka M. ‘The Structure of a N11A Mutant from the G-protein Domain of FeoB’ (2011) Acta Cryst., F67, 1511-5.
  23. Ash M.-R., Maher M. J., Guss J. M. and Jormakka M. ‘A Suite of Switch I and Switch II Mutant Structures from the G-protein Domain of FeoB’ (2011) Acta Cryst., D67, 973-80.
  24. Ash M.-R., Maher M. J., Guss J. M. and Jormakka M. ‘The Initiation of GTP Hydrolysis by the G-domain of FeoB: Insights from a Transition-State Complex Structure’ (2011) PLoS One, 6, e23355.
  25. Ash M.-R., Chong L. X., Maher M. J.#, Hinds M. G., Xiao Z. and Wedd A. G.# ‘Molecular Basis of the Cooperative Binding of Cu(I) and Cu(II) to the CopK protein from Cupriavidus metallidurans CH34’ (2011) Biochemistry., 50, 9237-47.  # joint corresponding author.
  26. Kilmartin J. R.#, Maher M. J.#, Krusong K., Noble C. J., Hanson G. R., Bernhardt P. V., Riley M. J. and Kappler U. ‘Insights into Structure and Function of the Active Site of SoxAX Cytochromes’ (2011) J. Biol. Chem., 28, 24872-81.  #joint primary author.\
  27. Ash M.-R., Guilfoyle A., Clarke R. J., Guss J. M., Maher M. J. and Jormakka M. ‘Potassium-activated GTPase Reaction in the G Protein Coupled Ferrous Iron Transporter B’ (2010) J. Biol. Chem., 285, 14594-602.
  28. Maher M. J., Akimoto S., Iwata M., Nagata K., Hori Y., Yoshida M., Yokoyama S., Iwata S., Yokoyama K. ‘Crystal Structure of the A(3)B(3) complex of V-ATPase from Thermus thermophilus.’ (2009) EMBO J., 28, 3771-3779.
  29. Guilfoyle A.#, Maher M. J.#, Rapp M., Clarke R., Harrop S. and Jormakka M. ‘Structural Basis of GDP Release and Gating in G Protein Coupled Fe2+’ (2009) EMBO J., 28, 2677-2685.  #joint primary author
  30. Andréll J., Hicks M. G., Palmer T., Carpenter E. P., Iwata S. and Maher M. J. ‘Crystal Structure of the Acid Induced Arginine Decarboxylase from Escherichia coli: Reversible Decamer Assembly Controls Enzyme Activity.’ (2009) Biochemistry, 48, 3915-3927.
  31. Chong L. X., Ash M-R., Maher M. J.#, Hinds M. G., Xiao Z., Wedd A. G.# ‘Unprecedented Binding Cooperativity between Cu(I) and Cu(II) in the Copper Resistance Protein CopK from Cupriavidus metallidurans CH34: Implications from Structural Studies by NMR Spectroscopy and X-Ray Crystallography.’ (2009) J. Am. Chem. Soc., 131, 3549-3564. #joint corresponding author
  32. Kouwen T. R., Andréll J., Schrijver R., Dubois J. Y., Maher M. J., Iwata S., Carpenter E. P., van Dijl J. M. ‘Thioredoxin A active-site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediates.’ (2008) J. Mol. Biol., 379, 520-534.
  33. Lee M., Maher M. J., Christopherson R. I. and Guss J. M. ‘Kinetic and Structural Analysis of the Mutant E. coli Dihydroorotases: a Flexible Loop Stabilises the Transition State’ (2007) Biochemistry, 46, 10538-10550.
  34. Lee M., Maher M. J. and Guss J. M. ‘Structure of the T109S Mutant of E. coli Dihydroorotase Complexed with the Inhibitor 5-Fluoroorotate: Catalytic Activity is Reflected by the Crystal Form.’ (2007) Acta Cryst., F63, 154-61.
  35. Lee M., Chan C. W., Graham S. C., Christopherson R. I., Guss J. M. and Maher M. J. ‘Structures of Ligand-Free and Inhibitor Complexes of Dihydroorotase from Escherichia coli: Implications for Loop Movement in Inhibitor Design’. (2007) J. Mol. Biol., 370, 812-825.
  36. Zhang L., Koay M., Maher M. J.#, Xiao Z., Wedd A. G.# ‘Intermolecular Transfer of Copper Ions from the CopC Protein of Pseudomonas syringae. Crystal Structures of Fully Loaded  Cu(I)Cu(II) Forms.’ (2006), J. Am. Chem. Soc., 128, 5834-5850. # joint corresponding author.
  37. Koay M., Zhang L., Yang B., Maher M. J., Xiao Z. and Wedd A. G. ‘The CopC Protein from Pseudomonas syringae: Intermolecular Transfer of Copper from both the Copper(I) and Copper(II) Sites.’ (2005), Inorg. Chem., 44, 5203-5205.
  38. Lee M., Chan C. W., Guss J. M., Christopherson R. I. and Maher M. J. ‘Dihydroorotase from Escherichia coli: Loop Movement and Cooperativity Between Subunits.’ (2005) J. Mol. Biol., 348, 523-533.
  39. Graham S. C., Maher M. J., Simmons W. H., Freeman H. C. and Guss J. M. ‘Structure of the E. coli Aminopeptidase P in complex with the Inhibitor Apstatin.’ (2004) Acta Cryst. D60, 1770-1779.
  40. Deane J. E., Ryan D. P., Sunde M., Maher M. J., Guss J. M., Visvader J. E. and Matthews J. M. ‘Tandem LIM Domains Provide Synergistic Binding in the LMO4:Ldb1 complex.’ (2004) EMBO J., 23, 3589-3598.
  41. Maher M. J., Ghosh M., Grunden A. M., Menon A. L., Adams M. W. W., Freeman H. C. and Guss J. M. ‘Structure of the Prolidase from Pyrococcus furiosus.’ (2004) Biochemistry, 43, 2771-2783.
  42. Maher M. J., Santini J. M., Pickering I. J., Prince R. C., Macy J. M. and George G. N. ‘X-ray Absorption Spectroscopy of Selenate Reductase.’ (2004) Inorg. Chem., 43, 402-404.
  43. Maher M. J., Cross M., Wilce M. C. J., Guss M. J. and Wedd A. G. ‘Metal-Substituted Derivatives of the Rubredoxin from Clostridium pasteurianum: Structures by X-ray Crystallography.’ (2004) Acta Cryst., D60, 298-303.
  44. Lee M., Maher M. J., Freeman H. C. and Guss J. M. ‘Auracyanin B Structure in Space Group P65.’ (2003) Acta Cryst., D59, 1545-1550.
  45. Deane J. E., Maher M. J., Langley D. B., Graham S. C., Visvader J. E., Guss J. M. and Matthews J. M. ‘Crystallization of FLINC4, an intramolecular LMO4-ldb1 complex.’ (2003) Acta Cryst., D59, 1484-1486.
  46. Maher M. J., Huang D. T. C., Guss J. M., Collyer C. A. and Christopherson R. I. ‘Crystallization of Hamster Dihydroorotase: Involvement of a Disulfide-Linked Tetrameric Form.’ (2003) Acta Cryst., D59, 381-384.
  47. Lee M., Willingham K., Langley D., Maher M. J., Cohen A. E., Ellis P. J., Kuchar J. A., Dooley D. M., Freeman H. C. and Guss J. M. ‘Crystallization of Pichia pastoris lysyl oxidase.’ (2002) Acta Cryst., D58, 2177-2179.
  48. Maher, M. J. and Macy, J. M. ‘Crystallisation and Preliminary X-ray Analysis of the Selenate Reductase from Thauera selenatis.’ (2002) Acta Cryst., D58, 706-708.
  49. Willingham, K., Maher, M. J., Grunden, A. M., Ghosh, M., Adams, M. W. W., Freeman, H. C. and Guss, J. M. ‘Crystallisation and Characterisation of the Prolidase from Pyrococcus furiosus.’ (2001) Acta Cryst., D57, 428-430.
  50. Bond, C. S., Blankenship, R. E., Freeman, H. C., Guss, J. M., Maher, M. J., Selvaraj, F. M., Wilce, M. C. J. and Willingham, K. M. ‘Crystal structure of Auracyanin, a ‘Blue’ Copper Protein from the Green Thermophilic Photosynthetic Bacterium Chloroflexus aurantiacus.’ (2001) J. Mol. Biol., 306, 47-67.
  51. Xiao, Z., Maher, M. J., Cross, M., Bond, C. S., Guss, J. M. and Wedd, A. G. ‘Mutation of the Surface Valine Residues 8 and 44 in the Rubredoxin from Clostridium pasteurianum.  Solvent Access Versus Structural Changes as Determinants of Reversible Potential.’  (2000) J. Bioinorg. Chem., 5, 75-84.
  52. Xiao Z., Lavery, M. J., Bond, A. M. and Wedd, A. G. ‘The Dependence of Reversible Potentials on the Form of Modification of Edge Plane Pyrolytic Graphite Electrodes in Voltammetric Studies on Rubredoxin and Ferredoxin from Clostridium Pasteurianum.’ (1999) Electrochemistry Communications, 1, 309-314.
  53. Maher, M. J., Xiao, Z., Wilce, M. C. J., Guss, J. M. and Wedd, A. G. ‘Rubredoxin from Clostridium pasteurianum: X-ray Crystal Structures of G10A, G43A and G10VG43A Mutant Proteins.  Mutation of Conserved Glycine 10 to Valine Causes the 9-10 Peptide Link to Invert.’ (1999)  Acta Cryst., D55, 962-968.
  54. Brereton, P. S., Maher, M. J., Tregloan, P. A. and Wedd, A. G. ‘Investigation of the Role of Surface Residues in the Ferredoxin from Clostridium pasteurianum.’ (1999)  Biophys. Acta., 1429, 307-316.
  55. Xiao, Z., Lavery, M. J., Ayhan, M., Scrofani, S. D. B., Wilce, M. C. J., Guss, J. M., Tregloan, P. A., George, G. N. and Wedd, A. G. ‘The Rubredoxin from Clostridium pasteurianum:  Mutation of the Iron Cysteinyl Ligands to Serine.  Crystal and Molecular Structures of Oxidised and Dithionite-Treated Forms of the Cys42Ser Mutant.’  (1998) J. Am. Chem. Soc., 120, 4135-4150.
  56. Ayhan M., Xiao Z., Lavery M. J., Hamer A. M., Scrofani S. D. B. and Wedd A. G. Rubredoxin from Clostridium pasteurianum: Mutation of the Conserved Cysteine and Glycine Residues. (1996) in Sulfur-Coordinated Transition Metal Complexes:  Biological and Industrial Significance; Matsumoto K., Stiefel E. I.; Eds.; ACS Symposium Series; American Chemical Society; Washington DC; 40-56.
  57. Ayhan, M., Xiao, Z., Lavery, M. J., Hamer, A. M., Nugent, K. W., Scrofani, S. D. B., Guss, J. M., and Wedd, A. G. ‘Rubredoxin from Clostridium pasteurianum: Mutation of the Conserved Glycine Residues 10 and 43 to Alanine and Valine.’ (1996) Inorg. Chem., 35, 5902-5991.
  58. Scrofani, S. D. B., Brereton, P. S., Hamer, A. M., Lavery, M. J., McDowell, S. G., Vincent, G. A., Brownlee, R. T. C., Hoogenraad, N. J., Sadek, M. and Wedd, A. G. ‘Comparison of Native and Mutant Proteins Provides a Sequence-Specific Assignment of the Cysteinyl Ligand Proton NMR Resonances in the 2[4Fe-4S] Ferredoxin from Clostridium pasteurianum.’ (1994) Biochemistry, 33, 14486-14495.

Other publication outputs

  1. Maher M. J., ‘The structure of an ‘alternative’ respiratory Complex I’ (2013) ESRF Highlights (invited contribution – ‘ESRF Highlights’ features scientific highlights from data collected at the European Synchrotron Research Facility during the previous year)