Search Results - "Birrell, James A."

Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer by Schuller, Jan M, Birrell, James A, Tanaka, Hideaki, Konuma, Tsuyoshi, Wulfhorst, Hannes, Cox, Nicholas, Schuller, Sandra K, Thiemann, Jacqueline, Lubitz, Wolfgang, Sétif, Pierre, Ikegami, Takahisa, Engel, Benjamin D, Kurisu, Genji, Nowaczyk, Marc M

“…Photosynthetic complex I enables cyclic electron flow around photosystem I, a regulatory mechanism for photosynthetic energy conversion. We report a…”
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Proton Coupled Electronic Rearrangement within the H‑Cluster as an Essential Step in the Catalytic Cycle of [FeFe] Hydrogenases by Sommer, Constanze, Adamska-Venkatesh, Agnieszka, Pawlak, Krzysztof, Birrell, James A, Rüdiger, Olaf, Reijerse, Edward J, Lubitz, Wolfgang

“…The active site of [FeFe] hydrogenases, the H-cluster, consists of a [4Fe–4S] cluster connected via a bridging cysteine to a [2Fe] complex carrying CO and CN–…”
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Caught in the Hinact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2‐stable State of [FeFe] Hydrogenase by Rodríguez‐Maciá, Patricia, Galle, Lisa M., Bjornsson, Ragnar, Lorent, Christian, Zebger, Ingo, Yoda, Yoshitaka, Cramer, Stephen P., DeBeer, Serena, Span, Ingrid, Birrell, James A.

“…[FeFe] hydrogenases are the most active H2 converting catalysts in nature, but their extreme oxygen sensitivity limits their use in technological applications…”
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Enantioselective Acylation of Silyl Ketene Acetals through Fluoride Anion-Binding Catalysis by Birrell, James A, Desrosiers, Jean-Nicolas, Jacobsen, Eric N

“…A highly enantioselective acylation of silyl ketene acetals with acyl fluorides has been developed to generate useful α,α-disubstituted butyrolactone products…”
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Spin Polarization Reveals the Coordination Geometry of the [FeFe] Hydrogenase Active Site in Its CO-Inhibited State by Reijerse, Edward, Birrell, James A, Lubitz, Wolfgang

“…The active site of [FeFe] hydrogenase features a binuclear iron cofactor Fe ADT(CO) (CN) , where ADT represents the bridging ligand aza-propane-dithiolate. The…”
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Reaction Coordinate Leading to H2 Production in [FeFe]-Hydrogenase Identified by Nuclear Resonance Vibrational Spectroscopy and Density Functional Theory by Pelmenschikov, Vladimir, Birrell, James A, Pham, Cindy C, Mishra, Nakul, Wang, Hongxin, Sommer, Constanze, Reijerse, Edward, Richers, Casseday P, Tamasaku, Kenji, Yoda, Yoshitaka, Rauchfuss, Thomas B, Lubitz, Wolfgang, Cramer, Stephen P

“…[FeFe]-hydrogenases are metalloenzymes that reversibly reduce protons to molecular hydrogen at exceptionally high rates. We have characterized the…”
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Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase from Thermotoga maritima by Chongdar, Nipa, Rodríguez-Maciá, Patricia, Reijerse, Edward J, Lubitz, Wolfgang, Ogata, Hideaki, Birrell, James A

“…[FeFe] hydrogenases are exceptionally active catalysts for the interconversion of molecular hydrogen with protons and electrons. Their active site, the…”
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Bioelectrocatalysis based on direct electron transfer of fungal pyrroloquinoline quinone-dependent dehydrogenase lacking the cytochrome domain by Takeda, Kouta, Kusuoka, Ryo, Birrell, James A., Yoshida, Makoto, Igarashi, Kiyohiko, Nakamura, Nobuhumi

“…•The PQQ domain can undergo direct bioelectrocatalysis without its cytochrome domain.•The AuE modified with SAM composed of 2-mercaptoethanol is suited for DET…”
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Investigating the function of [2Fe-2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential by Birrell, James A, Morina, Klaudia, Bridges, Hannah R, Friedrich, Thorsten, Hirst, Judy

“…NADH:quinone oxidoreductase (complex I) couples NADH oxidation and quinone reduction to proton translocation across an energy-transducing membrane. All…”
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His-Ligation to the [4Fe–4S] Subcluster Tunes the Catalytic Bias of [FeFe] Hydrogenase by Rodríguez-Maciá, Patricia, Kertess, Leonie, Burnik, Jan, Birrell, James A, Hofmann, Eckhard, Lubitz, Wolfgang, Happe, Thomas, Rüdiger, Olaf

“…[FeFe] hydrogenases interconvert H2 into protons and electrons reversibly and efficiently. The active site H-cluster is composed of two sites: a unique [2Fe]…”
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Structural insight on the mechanism of an electron-bifurcating [FeFe] hydrogenase by Furlan, Chris, Chongdar, Nipa, Gupta, Pooja, Lubitz, Wolfgang, Ogata, Hideaki, Blaza, James N, Birrell, James A

“…Electron bifurcation is a fundamental energy conservation mechanism in nature in which two electrons from an intermediate-potential electron donor are split so…”
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Truncation of subunit ND2 disrupts the threefold symmetry of the antiporter-like subunits in complex I from higher metazoans by Birrell, James A., Hirst, Judy

“…Three of the conserved, membrane-bound subunits in NADH:ubiquinone oxidoreductase (complex I) are related to one another, and to Mrp sodium-proton antiporters…”
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Reactions of the Flavin Mononucleotide in Complex I: A Combined Mechanism Describes NADH Oxidation Coupled to the Reduction of APAD+, Ferricyanide, or Molecular Oxygen by Birrell, James A, Yakovlev, Gregory, Hirst, Judy

“…NADH:ubiquinone oxidoreductase (complex I) is a complicated respiratory chain enzyme that conserves the energy from NADH oxidation, coupled to ubiquinone…”
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Spectroscopic Evidence of Reversible Disassembly of the [FeFe] Hydrogenase Active Site by Rodríguez-Maciá, Patricia, Reijerse, Edward, Lubitz, Wolfgang, Birrell, James A, Rüdiger, Olaf

“…[FeFe] hydrogenases are extremely active and efficient H2-converting biocatalysts. Their active site comprises a unique [2Fe] subcluster bonded to a canonical…”
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The mitochondrial-encoded subunits of respiratory complex I (NADH:ubiquinone oxidoreductase): identifying residues important in mechanism and disease by Bridges, Hannah R, Birrell, James A, Hirst, Judy

“…Complex I (NADH:ubiquinone oxidoreductase) is crucial to respiration in many aerobic organisms. The hydrophilic domain of complex I, containing nine or more…”
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Artificial Maturation of the Highly Active Heterodimeric [FeFe] Hydrogenase from Desulfovibrio desulfuricans ATCC 7757 by Birrell, James A., Wrede, Kathrin, Pawlak, Krzysztof, Rodriguez-Maciá, Patricia, Rüdiger, Olaf, Reijerse, Edward J., Lubitz, Wolfgang

“…Hydrogenases catalyze the reduction of protons and oxidation of molecular hydrogen with high turnover frequencies and low overpotentials under ambient…”
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The Spectroscopy of Nitrogenases by Van Stappen, Casey, Decamps, Laure, Bjornsson, Ragnar, Henthorn, Justin T, Birrell, James A, DeBeer, Serena

“…Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the biogeochemical nitrogen cycle. These enzymes utilize a two-component…”
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The catalytic cycle of [FeFe] hydrogenase: A tale of two sites by Birrell, James A., Rodríguez-Maciá, Patricia, Reijerse, Edward J., Martini, Maria Alessandra, Lubitz, Wolfgang

“…[Display omitted] •[FeFe] hydrogenases use earth abundant metals for efficient hydrogen activation.•Understanding their catalytic mechanism may help synthesise…”
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Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates by Birrell, James A, Pelmenschikov, Vladimir, Mishra, Nakul, Wang, Hongxin, Yoda, Yoshitaka, Tamasaku, Kenji, Rauchfuss, Thomas B, Cramer, Stephen P, Lubitz, Wolfgang, DeBeer, Serena

“…[FeFe] hydrogenases are extremely active H2-converting enzymes. Their mechanism remains highly controversial, in particular, the nature of the one-electron and…”
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Redox‐Polymer‐Based High‐Current‐Density Gas‐Diffusion H2‐Oxidation Bioanode Using [FeFe] Hydrogenase from Desulfovibrio desulfuricans in a Membrane‐free Biofuel Cell by Szczesny, Julian, Birrell, James A., Conzuelo, Felipe, Lubitz, Wolfgang, Ruff, Adrian, Schuhmann, Wolfgang

“…The incorporation of highly active but also highly sensitive catalysts (e.g. the [FeFe] hydrogenase from Desulfovibrio desulfuricans) in biofuel cells is still…”
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