Dr James Birrell

Sanchez, MLK., Wiley, S., Reijerse, E., Lubitz, W., Birrell, JA. and Dyer, RB., (2022). Time-Resolved Infrared Spectroscopy Reveals the pH-Independence of the First Electron Transfer Step in the [FeFe] Hydrogenase Catalytic Cycle.. Journal of Physical Chemistry Letters. 13 (25), 5986-5990

Chatterjee, S., Harden, I., Bistoni, G., Castillo, RG., Chabbra, S., van Gastel, M., Schnegg, A., Bill, E., Birrell, JA., Morandi, B., Neese, F. and DeBeer, S., (2022). A Combined Spectroscopic and Computational Study on the Mechanism of Iron-Catalyzed Aminofunctionalization of Olefins Using Hydroxylamine Derived N-O Reagent as the "Amino" Source and "Oxidant".. Journal of the American Chemical Society. 144 (6), 2637-2656

Furlan, C., Chongdar, N., Gupta, P., Lubitz, W., Ogata, H., Blaza, JN. and Birrell, JA., (2022). Structural insight on the mechanism of an electron-bifurcating [FeFe] hydrogenase.. eLife. 11, e79361-

Becker, JM., Lielpetere, A., Szczesny, J., Junqueira, JRC., Rodríguez-Maciá, P., Birrell, JA., Conzuelo, F. and Schuhmann, W., (2022). Bioelectrocatalytic CO₂ Reduction by Redox Polymer-Wired Carbon Monoxide Dehydrogenase Gas Diffusion Electrodes. ACS Applied Materials and Interfaces. 14 (41), 46421-46426

Lielpetere, A., Becker, JM., Szczesny, J., Conzuelo, F., Ruff, A., Birrell, J., Lubitz, W. and Schuhmann, W., (2022). Enhancing the catalytic current response of H₂ oxidation gas diffusion bioelectrodes using an optimized viologen‐based redox polymer and [NiFe] hydrogenase. Electrochemical Science Advances. 2 (4)

Pelmenschikov, V., Birrell, JA., Gee, LB., Richers, CP., Reijerse, EJ., Wang, H., Arragain, S., Mishra, N., Yoda, Y., Matsuura, H., Li, L., Tamasaku, K., Rauchfuss, TB., Lubitz, W. and Cramer, SP., (2021). Vibrational Perturbation of the [FeFe] Hydrogenase H-Cluster Revealed by ¹³C²H-ADT Labeling. Journal of the American Chemical Society. 143 (22), 8237-8243

Birrell, JA., Rodríguez-Maciá, P., Reijerse, EJ., Martini, MA. and Lubitz, W., (2021). The catalytic cycle of [FeFe] hydrogenase: A tale of two sites. Coordination Chemistry Reviews. 449, 214191-214191

Birrell, JA., Rodríguez-Maciá, P. and Hery-Barranco, A., (2021). A Beginner’s Guide to Thermodynamic Modelling of [FeFe] Hydrogenase. Catalysts. 11 (2), 238-238

Hardt, S., Stapf, S., Filmon, DT., Birrell, JA., Rüdiger, O., Fourmond, V., Léger, C. and Plumeré, N., (2021). Reversible H₂ Oxidation and Evolution by Hydrogenase Embedded in a Redox Polymer Film.. Nature Catalysis. 4 (3), 251-258

Rosenbach, H., Walla, E., Cutsail, GE., Birrell, JA., Pascual-Ortiz, M., DeBeer, S., Fleig, U. and Span, I., (2021). The Asp1 pyrophosphatase from S. pombe hosts a [2Fe-2S]²⁺ cluster in vivo.. Journal of Biological Inorganic Chemistry. 26 (1), 93-108

Martini, MA., Rüdiger, O., Breuer, N., Nöring, B., DeBeer, S., Rodríguez-Maciá, P. and Birrell, JA., (2021). The Nonphysiological Reductant Sodium Dithionite and [FeFe] Hydrogenase: Influence on the Enzyme Mechanism.. Journal of the American Chemical Society. 143 (43), 18159-18171

Takeda, K., Kusuoka, R., Birrell, JA., Yoshida, M., Igarashi, K. and Nakamura, N., (2020). Bioelectrocatalysis based on direct electron transfer of fungal pyrroloquinoline quinone-dependent dehydrogenase lacking the cytochrome domain. Electrochimica Acta. 359, 136982-136982

Szczesny, J., Birrell, JA., Conzuelo, F., Lubitz, W., Ruff, A. and Schuhmann, W., (2020). Redox‐Polymer‐Based High‐Current‐Density Gas‐Diffusion H₂‐Oxidation Bioanode Using [FeFe] Hydrogenase from Desulfovibrio desulfuricans in a Membrane‐free Biofuel Cell. Angewandte Chemie International Edition. 59 (38), 16506-16510

Rodríguez-Maciá, P., Breuer, N., DeBeer, S. and Birrell, JA., (2020). Insight into the Redox Behavior of the [4Fe–4S] Subcluster in [FeFe] Hydrogenases. ACS Catalysis. 10 (21), 13084-13095

Birrell, JA., Pelmenschikov, V., Mishra, N., Wang, H., Yoda, Y., Tamasaku, K., Rauchfuss, TB., Cramer, SP., Lubitz, W. and DeBeer, S., (2020). Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates. Journal of the American Chemical Society. 142 (1), 222-232

Van Stappen, C., Decamps, L., Cutsail, GE., Bjornsson, R., Henthorn, JT., Birrell, JA. and DeBeer, S., (2020). The Spectroscopy of Nitrogenases. Chemical Reviews. 120 (12), 5005-5081

Oughli, AA., Hardt, S., Rüdiger, O., Birrell, JA. and Plumeré, N., (2020). Reactivation of sulfide-protected [FeFe] hydrogenase in a redox-active hydrogel. Chemical Communications. 56 (69), 9958-9961

Jagilinki, BP., Ilic, S., Trncik, C., Tyryshkin, AM., Pike, DH., Lubitz, W., Bill, E., Einsle, O., Birrell, JA., Akabayov, B., Noy, D. and Nanda, V., (2020). In Vivo Biogenesis of a De Novo Designed Iron–Sulfur Protein. ACS Synthetic Biology. 9 (12), 3400-3407

Reijerse, E., Birrell, JA. and Lubitz, W., (2020). Spin Polarization Reveals the Coordination Geometry of the [FeFe] Hydrogenase Active Site in Its CO-Inhibited State. The Journal of Physical Chemistry Letters. 11 (12), 4597-4602

Sanchez, MLK., Konecny, SE., Narehood, SM., Reijerse, EJ., Lubitz, W., Birrell, JA. and Dyer, RB., (2020). The Laser-Induced Potential Jump: A Method for Rapid Electron Injection into Oxidoreductase Enzymes. The Journal of Physical Chemistry B. 124 (40), 8750-8760

Rodríguez‐Maciá, P., Galle, LM., Bjornsson, R., Lorent, C., Zebger, I., Yoda, Y., Cramer, SP., DeBeer, S., Span, I. and Birrell, JA., (2020). Caught in the H_inact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O₂‐stable State of [FeFe] Hydrogenase. Angewandte Chemie International Edition. 59 (38), 16786-16794

Chongdar, N., Pawlak, K., Rüdiger, O., Reijerse, EJ., Rodríguez-Maciá, P., Lubitz, W., Birrell, JA. and Ogata, H., (2020). Spectroscopic and biochemical insight into an electron-bifurcating [FeFe] hydrogenase. JBIC Journal of Biological Inorganic Chemistry. 25 (1), 135-149

Reijerse, EJ., Pelmenschikov, V., Birrell, JA., Richers, CP., Kaupp, M., Rauchfuss, TB., Cramer, SP. and Lubitz, W., (2019). Asymmetry in the Ligand Coordination Sphere of the [FeFe] Hydrogenase Active Site Is Reflected in the Magnetic Spin Interactions of the Aza-propanedithiolate Ligand. The Journal of Physical Chemistry Letters. 10 (21), 6794-6799

Sanchez, MLK., Sommer, C., Reijerse, E., Birrell, JA., Lubitz, W. and Dyer, RB., (2019). Investigating the Kinetic Competency of CrHydA1 [FeFe] Hydrogenase Intermediate States via Time-Resolved Infrared Spectroscopy. Journal of the American Chemical Society. 141 (40), 16064-16070

Rodríguez-Maciá, P., Kertess, L., Burnik, J., Birrell, JA., Hofmann, E., Lubitz, W., Happe, T. and Rüdiger, O., (2019). His-Ligation to the [4Fe–4S] Subcluster Tunes the Catalytic Bias of [FeFe] Hydrogenase. Journal of the American Chemical Society. 141 (1), 472-481

Schuller, JM., Birrell, JA., Tanaka, H., Konuma, T., Wulfhorst, H., Cox, N., Schuller, SK., Thiemann, J., Lubitz, W., Sétif, P., Ikegami, T., Engel, BD., Kurisu, G. and Nowaczyk, MM., (2019). Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. Science. 363 (6424), 257-260

Rodríguez-Maciá, P., Reijerse, EJ., van Gastel, M., DeBeer, S., Lubitz, W., Rüdiger, O. and Birrell, JA., (2018). Sulfide Protects [FeFe] Hydrogenases From O₂. Journal of the American Chemical Society. 140 (30), 9346-9350

Oughli, AA., Vélez, M., Birrell, JA., Schuhmann, W., Lubitz, W., Plumeré, N. and Rüdiger, O., (2018). Viologen-modified electrodes for protection of hydrogenases from high potential inactivation while performing H₂oxidation at low overpotential. Dalton Transactions. 47 (31), 10685-10691

Chongdar, N., Birrell, JA., Pawlak, K., Sommer, C., Reijerse, EJ., Rüdiger, O., Lubitz, W. and Ogata, H., (2018). Unique Spectroscopic Properties of the H-Cluster in a Putative Sensory [FeFe] Hydrogenase. Journal of the American Chemical Society. 140 (3), 1057-1068

Rodríguez‐Maciá, P., Birrell, JA., Lubitz, W. and Rüdiger, O., (2017). Electrochemical Investigations on the Inactivation of the [FeFe] Hydrogenase from Desulfovibrio desulfuricans by O₂ or Light under Hydrogen‐Producing Conditions. ChemPlusChem. 82 (4), 540-545

Birrell, JA., Rüdiger, O., Reijerse, EJ. and Lubitz, W., (2017). Semisynthetic Hydrogenases Propel Biological Energy Research into a New Era. Joule. 1 (1), 61-76

Pelmenschikov, V., Birrell, JA., Pham, CC., Mishra, N., Wang, H., Sommer, C., Reijerse, E., Richers, CP., Tamasaku, K., Yoda, Y., Rauchfuss, TB., Lubitz, W. and Cramer, SP., (2017). Reaction Coordinate Leading to H₂ Production in [FeFe]-Hydrogenase Identified by Nuclear Resonance Vibrational Spectroscopy and Density Functional Theory. Journal of the American Chemical Society. 139 (46), 16894-16902

Rodríguez-Maciá, P., Pawlak, K., Rüdiger, O., Reijerse, EJ., Lubitz, W. and Birrell, JA., (2017). Intercluster Redox Coupling Influences Protonation at the H-cluster in [FeFe] Hydrogenases. Journal of the American Chemical Society. 139 (42), 15122-15134

Rodríguez-Maciá, P., Reijerse, E., Lubitz, W., Birrell, JA. and Rüdiger, O., (2017). Spectroscopic Evidence of Reversible Disassembly of the [FeFe] Hydrogenase Active Site. The Journal of Physical Chemistry Letters. 8 (16), 3834-3839

Sommer, C., Adamska-Venkatesh, A., Pawlak, K., Birrell, JA., Rüdiger, O., Reijerse, EJ. and Lubitz, W., (2017). Proton Coupled Electronic Rearrangement within the H-Cluster as an Essential Step in the Catalytic Cycle of [FeFe] Hydrogenases. Journal of the American Chemical Society. 139 (4), 1440-1443

Birrell, JA., Laurich, C., Reijerse, EJ., Ogata, H. and Lubitz, W., (2016). Importance of Hydrogen Bonding in Fine Tuning the [2Fe-2S] Cluster Redox Potential of HydC from Thermotoga maritima. Biochemistry. 55 (31), 4344-4355

Birrell, JA., Wrede, K., Pawlak, K., Rodriguez‐Maciá, P., Rüdiger, O., Reijerse, EJ. and Lubitz, W., (2016). Artificial Maturation of the Highly Active Heterodimeric [FeFe] Hydrogenase from Desulfovibrio desulfuricans ATCC 7757. Israel Journal of Chemistry. 56 (9-10), 852-863

Kutin, Y., Srinivas, V., Fritz, M., Kositzki, R., Shafaat, HS., Birrell, J., Bill, E., Haumann, M., Lubitz, W., Högbom, M., Griese, JJ. and Cox, N., (2016). Divergent assembly mechanisms of the manganese/iron cofactors in R2lox and R2c proteins. Journal of Inorganic Biochemistry. 162, 164-177

Fourmond, V., Stapf, S., Li, H., Buesen, D., Birrell, J., Rüdiger, O., Lubitz, W., Schuhmann, W., Plumeré, N. and Léger, C., (2015). Mechanism of Protection of Catalysts Supported in Redox Hydrogel Films. Journal of the American Chemical Society. 137 (16), 5494-5505

Birrell, JA., Morina, K., Bridges, HR., Friedrich, T. and Hirst, J., (2013). Investigating the function of [2Fe–2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential. Biochemical Journal. 456 (1), 139-146

Birrell, JA. and Hirst, J., (2013). Investigation of NADH Binding, Hydride Transfer, and NAD⁺ Dissociation during NADH Oxidation by Mitochondrial Complex I Using Modified Nicotinamide Nucleotides. Biochemistry. 52 (23), 4048-4055

Birrell, JA. and Jacobsen, EN., (2013). A Practical Method for the Synthesis of Highly Enantioenriched trans-1,2-Amino Alcohols. Organic Letters. 15 (12), 2895-2897

Birrell, JA., King, MS. and Hirst, J., (2011). A ternary mechanism for NADH oxidation by positively charged electron acceptors, catalyzed at the flavin site in respiratory complex I. FEBS Letters. 585 (14), 2318-2322

Bridges, HR., Birrell, JA. and Hirst, J., (2011). The mitochondrial-encoded subunits of respiratory complex I (NADH:ubiquinone oxidoreductase): identifying residues important in mechanism and disease. Biochemical Society Transactions. 39 (3), 799-806

Birrell, JA., Desrosiers, J-N. and Jacobsen, EN., (2011). Enantioselective Acylation of Silyl Ketene Acetals through Fluoride Anion-Binding Catalysis. Journal of the American Chemical Society. 133 (35), 13872-13875

Birrell, JA. and Hirst, J., (2010). Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter‐like subunits in complex I from higher metazoans. FEBS Letters. 584 (19), 4247-4252

Birrell, JA., Yakovlev, G. and Hirst, J., (2009). Reactions of the Flavin Mononucleotide in Complex I: A Combined Mechanism Describes NADH Oxidation Coupled to the Reduction of APAD⁺, Ferricyanide, or Molecular Oxygen. Biochemistry. 48 (50), 12005-12013