@misc{McKennaLeimkuehlerHerteretal.2015,
  author    = {McKenna, Shane M. and Leimk{\"u}hler, Silke and Herter, Susanne and Turner, Nicholas J. and Carnell, Andrew J.},
  title     = {Enzyme cascade reactions},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-102271},
  pages     = {3271 -- 3275},
  year      = {2015},
  abstract  = {A one-pot tandem enzyme reaction using galactose oxidase M3-5 and aldehyde oxidase PaoABC was used to convert hydroxymethylfurfural (HMF) to the pure bioplastics precursor FDCA in 74\% isolated yield. A range of alcohols was also converted to carboxylic acids in high yield under mild conditions.},
  language  = {en}
}
@article{BechiHerterMcKennaetal.2014,
  author    = {Bechi, Beatrice and Herter, Susanne and McKenna, Shane and Riley, Christopher and Leimk{\"u}hler, Silke and Turner, Nicholas J. and Carnell, Andrew J.},
  title     = {Catalytic bio-chemo and bio-bio tandem oxidation reactions for amide and carboxylic acid synthesis},
  series = {Green chemistry : an international journal and green chemistry resource},
  volume    = {16},
  journal   = {Green chemistry : an international journal and green chemistry resource},
  number    = {10},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1463-9262},
  doi       = {10.1039/c4gc01321b},
  pages     = {4524 -- 4529},
  year      = {2014},
  abstract  = {A catalytic toolbox for three different water-based one-pot cascades to convert aryl alcohols to amides and acids and cyclic amines to lactams, involving combination of oxidative enzymes (monoamine oxidase, xanthine dehydrogenase, galactose oxidase and laccase) and chemical oxidants (TBHP or Cul(cat)/H2O2) at mild temperatures, is presented. Mutually compatible conditions were found to afford products in good to excellent yields.},
  language  = {en}
}
@article{HerterMcKennaFrazeretal.2015,
  author    = {Herter, Susanne and McKenna, Shane M. and Frazer, Andrew R. and Leimk{\"u}hler, Silke and Carnell, Andrew J. and Turner, Nicholas J.},
  title     = {Galactose Oxidase Variants for the Oxidation of Amino Alcohols in Enzyme Cascade Synthesis},
  series = {ChemCatChem : heterogeneous \& homogeneous \& bio- \& nano-catalysis ; a journal of ChemPubSoc Europe},
  volume    = {7},
  journal   = {ChemCatChem : heterogeneous \& homogeneous \& bio- \& nano-catalysis ; a journal of ChemPubSoc Europe},
  number    = {15},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1867-3880},
  doi       = {10.1002/cctc.201500218},
  pages     = {2313 -- 2317},
  year      = {2015},
  abstract  = {The use of selected engineered galactose oxidase (GOase) variants for the oxidation of amino alcohols to aldehydes under mild conditions in aqueous systems is reported. GOase variant F-2 catalyses the regioselective oxidation of N-carbobenzyloxy (Cbz)-protected 3-amino-1,2-propanediol to the corresponding -hydroxyaldehyde which was then used in an aldolase reaction. Another variant, M3-5, was found to exhibit activity towards free and N-Cbz-protected aliphatic and aromatic amino alcohols allowing the synthesis of lactams such as 3,4-dihydronaphthalen-1(2H)-one, 2-pyrrolidone and valerolactam in one-pot tandem reactions with xanthine dehydrogenase (XDH) or aldehyde oxidase (PaoABC).},
  language  = {en}
}
@article{McKennaLeimkuehlerHerteretal.2015,
  author    = {McKenna, Shane M. and Leimk{\"u}hler, Silke and Herter, Susanne and Turner, Nicholas J. and Carnell, Andrew J.},
  title     = {Enzyme cascade reactions: synthesis of furandicarboxylic acid (FDCA) and carboxylic acids using oxidases in tandem},
  series = {Green chemistry : an international journal and green chemistry resource},
  volume    = {17},
  journal   = {Green chemistry : an international journal and green chemistry resource},
  number    = {6},
  publisher = {Royal Society of Chemistry},
  address   = {Cambridge},
  issn      = {1463-9262},
  doi       = {10.1039/c5gc00707k},
  pages     = {3271 -- 3275},
  year      = {2015},
  abstract  = {A one-pot tandem enzyme reaction using galactose oxidase M3-5 and aldehyde oxidase PaoABC was used to convert hydroxymethylfurfural (HMF) to the pure bioplastics precursor FDCA in 74\% isolated yield. A range of alcohols was also converted to carboxylic acids in high yield under mild conditions.},
  language  = {en}
}
@article{MitznerRehanekKernetal.2013,
  author    = {Mitzner, Rolf and Rehanek, Jens and Kern, Jan and Gul, Sheraz and Hattne, Johan and Taguchi, Taketo and Alonso-Mori, Roberto and Tran, Rosalie and Weniger, Christian and Schr{\"o}der, Henning and Quevedo, Wilson and Laksmono, Hartawan and Sierra, Raymond G. and Han, Guangye and Lassalle-Kaiser, Benedikt and Koroidov, Sergey and Kubicek, Katharina and Schreck, Simon and Kunnus, Kristjan and Brzhezinskaya, Maria and Firsov, Alexander and Minitti, Michael P. and Turner, Joshua J. and M{\"o}ller, Stefan and Sauter, Nicholas K. and Bogan, Michael J. and Nordlund, Dennis and Schlotter, William F. and Messinger, Johannes and Borovik, Andrew S. and Techert, Simone and de Groot, Frank M. F. and F{\"o}hlisch, Alexander and Erko, Alexei and Bergmann, Uwe and Yachandra, Vittal K. and Wernet, Philippe and Yano, Junko},
  title     = {L-edge x-ray absorption spectroscopy of dilute systems relevant to metalloproteins using an X-ray free-electron laser},
  series = {The journal of physical chemistry letters},
  volume    = {4},
  journal   = {The journal of physical chemistry letters},
  number    = {21},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {1948-7185},
  doi       = {10.1021/jz401837f},
  pages     = {3641 -- 3647},
  year      = {2013},
  abstract  = {L-edge spectroscopy of 3d transition metals provides important electronic structure information and has been used in many fields. However, the use of this method for studying dilute aqueous systems, such as metalloenzymes, has not been prevalent because of severe radiation damage and the lack of suitable detection systems. Here we present spectra from a dilute Mn aqueous solution using a high-transmission zone-plate spectrometer at the Linac Coherent Light Source (LCLS). The spectrometer has been optimized for discriminating the Mn L-edge signal from the overwhelming 0 K-edge background that arises from water and protein itself, and the ultrashort LCLS X-ray pulses can outrun X-ray induced damage. We show that the deviations of the partial-fluorescence yield-detected spectra from the true absorption can be well modeled using the state-dependence of the fluorescence yield, and discuss implications for the application of our concept to biological samples.},
  language  = {en}
}
@misc{BechiHerterMcKennaetal.2014,
  author    = {Bechi, Beatrice and Herter, Susanne and McKenna, Shane and Riley, Christopher and Leimk{\"u}hler, Silke and Turner, Nicholas J. and Carnell, Andrew J.},
  title     = {Catalytic bio-chemo and bio-bio tandem oxidation reactions for amide and carboxylic acid synthesis},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-99414},
  year      = {2014},
  abstract  = {A catalytic toolbox for three different water-based one-pot cascades to convert aryl alcohols to amides and acids and cyclic amines to lactams, involving combination of oxidative enzymes (monoamine oxidase, xanthine dehydrogenase, galactose oxidase and laccase) and chemical oxidants (TBHP or CuI(cat)/H2O2) at mild temperatures, is presented. Mutually compatible conditions were found to afford products in good to excellent yields.},
  language  = {en}
}