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  1. Article ; Online: Discovery of lignin-transforming bacteria and enzymes in thermophilic environments using stable isotope probing.

    Levy-Booth, David J / Navas, Laura E / Fetherolf, Morgan M / Liu, Li-Yang / Dalhuisen, Thomas / Renneckar, Scott / Eltis, Lindsay D / Mohn, William W

    The ISME journal

    2022  Volume 16, Issue 8, Page(s) 1944–1956

    Abstract: Characterizing microorganisms and enzymes involved in lignin biodegradation in thermal ecosystems can identify thermostable biocatalysts. We integrated stable isotope probing (SIP), genome-resolved metagenomics, and enzyme characterization to investigate ...

    Abstract Characterizing microorganisms and enzymes involved in lignin biodegradation in thermal ecosystems can identify thermostable biocatalysts. We integrated stable isotope probing (SIP), genome-resolved metagenomics, and enzyme characterization to investigate the degradation of high-molecular weight,
    MeSH term(s) Bacteria/genetics ; Bacteria/metabolism ; Gammaproteobacteria/metabolism ; Isotopes/metabolism ; Lignin/metabolism ; Microbiota ; Tandem Mass Spectrometry
    Chemical Substances Isotopes ; Lignin (9005-53-2)
    Language English
    Publishing date 2022-05-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2406536-5
    ISSN 1751-7370 ; 1751-7362
    ISSN (online) 1751-7370
    ISSN 1751-7362
    DOI 10.1038/s41396-022-01241-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Bonn / Germany

    Z 7773: Show issues

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  2. Article: Catabolism of Alkylphenols in

    Levy-Booth, David J / Fetherolf, Morgan M / Stewart, Gordon R / Liu, Jie / Eltis, Lindsay D / Mohn, William W

    Frontiers in microbiology

    2019  Volume 10, Page(s) 1862

    Abstract: The bacterial catabolism of aromatic compounds has considerable promise to convert lignin depolymerization products to commercial chemicals. Alkylphenols are a key class of depolymerization products whose catabolism is not well-elucidated. We ... ...

    Abstract The bacterial catabolism of aromatic compounds has considerable promise to convert lignin depolymerization products to commercial chemicals. Alkylphenols are a key class of depolymerization products whose catabolism is not well-elucidated. We isolated
    Language English
    Publishing date 2019-08-20
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2587354-4
    ISSN 1664-302X
    ISSN 1664-302X
    DOI 10.3389/fmicb.2019.01862
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Characterization of alkylguaiacol-degrading cytochromes P450 for the biocatalytic valorization of lignin.

    Fetherolf, Morgan M / Levy-Booth, David J / Navas, Laura E / Liu, Jie / Grigg, Jason C / Wilson, Andrew / Katahira, Rui / Beckham, Gregg T / Mohn, William W / Eltis, Lindsay D

    Proceedings of the National Academy of Sciences of the United States of America

    2020  Volume 117, Issue 41, Page(s) 25771–25778

    Abstract: Cytochrome P450 enzymes have tremendous potential as industrial biocatalysts, including in biological lignin valorization. Here, we describe P450s that catalyze ... ...

    Abstract Cytochrome P450 enzymes have tremendous potential as industrial biocatalysts, including in biological lignin valorization. Here, we describe P450s that catalyze the
    MeSH term(s) Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biocatalysis ; Biodegradation, Environmental ; Cytochrome P-450 Enzyme System/chemistry ; Cytochrome P-450 Enzyme System/genetics ; Cytochrome P-450 Enzyme System/metabolism ; Guaiacol/chemistry ; Guaiacol/metabolism ; Kinetics ; Lignin/chemistry ; Lignin/metabolism ; Rhodococcus/chemistry ; Rhodococcus/enzymology ; Rhodococcus/genetics ; Rhodococcus/metabolism ; Substrate Specificity
    Chemical Substances Bacterial Proteins ; Guaiacol (6JKA7MAH9C) ; Lignin (9005-53-2) ; Cytochrome P-450 Enzyme System (9035-51-2)
    Language English
    Publishing date 2020-09-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1916349117
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  4. Article: A thermostable laccase from Thermus sp. 2.9 and its potential for delignification of Eucalyptus biomass.

    Navas, Laura E / Martínez, Fernando D / Taverna, María E / Fetherolf, Morgan M / Eltis, Lindsay D / Nicolau, Verónica / Estenoz, Diana / Campos, Eleonora / Benintende, Graciela B / Berretta, Marcelo F

    AMB Express

    2019  Volume 9, Issue 1, Page(s) 24

    Abstract: Laccases are multicopper oxidases that are being studied for their potential application in pretreatment strategies of lignocellulosic feedstocks for bioethanol production. Here, we report the expression and characterization of a predicted laccase (LAC_2. ...

    Abstract Laccases are multicopper oxidases that are being studied for their potential application in pretreatment strategies of lignocellulosic feedstocks for bioethanol production. Here, we report the expression and characterization of a predicted laccase (LAC_2.9) from the thermophilic bacterial strain Thermus sp. 2.9 and investigate its capacity to delignify lignocellulosic biomass. The purified enzyme displayed a blue color typical of laccases, showed strict copper dependence and retained 80% of its activity after 16 h at 70 °C. At 60 °C, the enzyme oxidized 2,2'-azino-di-(3-ethylbenzthiazoline sulfonate) (ABTS) and 2,6-dimethoxyphenol (DMP) at optimal pH of 5 and 6, respectively. LAC_2.9 had higher substrate specificity (k
    Language English
    Publishing date 2019-02-12
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2621432-5
    ISSN 2191-0855
    ISSN 2191-0855
    DOI 10.1186/s13568-019-0748-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.

    Fetherolf, Morgan M / Boyd, Stefanie D / Taylor, Alexander B / Kim, Hee Jong / Wohlschlegel, James A / Blackburn, Ninian J / Hart, P John / Winge, Dennis R / Winkler, Duane D

    The Journal of biological chemistry

    2017  Volume 292, Issue 29, Page(s) 12025–12040

    Abstract: Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering ...

    Abstract Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond. Here, we present structural, spectroscopic, and cell-based data supporting a novel copper-induced mechanism for Sod1 activation. Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on immature Sod1. Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into the Sod1 active site. Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment.
    MeSH term(s) Amino Acid Substitution ; Apoenzymes/chemistry ; Apoenzymes/genetics ; Apoenzymes/metabolism ; Binding Sites ; Copper/metabolism ; Crystallography, X-Ray ; Cysteine/metabolism ; Cystine/metabolism ; Enzyme Activation ; Enzyme Stability ; Humans ; Ligands ; Models, Molecular ; Molecular Chaperones/chemistry ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Mutagenesis, Site-Directed ; Mutation ; Oxidation-Reduction ; Protein Conformation ; Protein Interaction Domains and Motifs ; Protein Processing, Post-Translational ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Superoxide Dismutase/chemistry ; Superoxide Dismutase/genetics ; Superoxide Dismutase/metabolism
    Chemical Substances Apoenzymes ; CCS1 protein, S cerevisiae ; Ligands ; Molecular Chaperones ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins ; Cystine (48TCX9A1VT) ; Copper (789U1901C5) ; LYS7 protein, S cerevisiae (EC 1.15.1.1) ; Superoxide Dismutase (EC 1.15.1.1) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2017-05-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M117.775981
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

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