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Structural Basis of Stereospecificity in the Bacterial Enzymatic Cleavage of ß-Aryl Ether Bonds in Lignin.
Helmich, Kate E; Pereira, Jose Henrique; Gall, Daniel L; Heins, Richard A; McAndrew, Ryan P; Bingman, Craig; Deng, Kai; Holland, Keefe C; Noguera, Daniel R; Simmons, Blake A; Sale, Kenneth L; Ralph, John; Donohue, Timothy J; Adams, Paul D; Phillips, George N.
Afiliação
  • Helmich KE; From the Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, the United States Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726.
  • Pereira JH; the Joint BioEnergy Institute, Emeryville, California 94608, the Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
  • Gall DL; the United States Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726, the Departments of Civil and Environmental Engineering and.
  • Heins RA; the Joint BioEnergy Institute, Emeryville, California 94608, the Biological and Engineering Sciences Center, Sandia National Laboratories, Livermore, California 94551.
  • McAndrew RP; the Joint BioEnergy Institute, Emeryville, California 94608, the Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720.
  • Bingman C; From the Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706.
  • Deng K; the Joint BioEnergy Institute, Emeryville, California 94608, the Biological and Engineering Sciences Center, Sandia National Laboratories, Livermore, California 94551.
  • Holland KC; the Joint BioEnergy Institute, Emeryville, California 94608, the Biological and Engineering Sciences Center, Sandia National Laboratories, Livermore, California 94551.
  • Noguera DR; the United States Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726, the Departments of Civil and Environmental Engineering and.
  • Simmons BA; the Joint BioEnergy Institute, Emeryville, California 94608, the Biological and Engineering Sciences Center, Sandia National Laboratories, Livermore, California 94551.
  • Sale KL; the Joint BioEnergy Institute, Emeryville, California 94608, the Biological and Engineering Sciences Center, Sandia National Laboratories, Livermore, California 94551.
  • Ralph J; From the Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, the United States Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726.
  • Donohue TJ; the United States Department of Energy Great Lakes Bioenergy Research Center, Wisconsin Energy Institute, University of Wisconsin, Madison, Wisconsin 53726, Bacteriology, University of Wisconsin, Madison, Wisconsin 53706, tdonohue@bact.wisc.edu.
  • Adams PD; the Joint BioEnergy Institute, Emeryville, California 94608, the Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, the Department of Bioengineering, University of California, Berkeley, California 94720, and pdadams@lbl.gov.
  • Phillips GN; the Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77251 georgep@rice.edu.
J Biol Chem ; 291(10): 5234-46, 2016 Mar 04.
Article em En | MEDLINE | ID: mdl-26637355
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxirredutases / Proteínas de Bactérias / Domínio Catalítico / Lignina Idioma: En Revista: J Biol Chem Ano de publicação: 2016 Tipo de documento: Article
Texto completo
Imprimir
XML
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Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oxirredutases / Proteínas de Bactérias / Domínio Catalítico / Lignina Idioma: En Revista: J Biol Chem Ano de publicação: 2016 Tipo de documento: Article