Výsledky vyhledávání - "George H. Gauss"

Distinct properties underlie flavin-based electron bifurcation in a novel electron transfer flavoprotein FixAB from Rhodopseudomonas palustris

Autor: H. Diessel Duan, John W. Peters, Paul W. King, Carolyn E. Lubner, George H. Gauss, Brian Bothner, Monika Tokmina-Lukaszewska, Anne-Frances Miller

Publikováno v: Journal of Biological Chemistry. 293:4688-4701

A newly recognized third fundamental mechanism of energy conservation in biology, electron bifurcation, uses free energy from exergonic redox reactions to drive endergonic redox reactions. Flavin-based electron bifurcation furnishes low-potential ele

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::daed8320371ff7e9fb63e25ec045b109
https://doi.org/10.1074/jbc.ra117.000707

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Structure-Based Mechanism for Oxidative Decarboxylation Reactions Mediated by Amino Acids and Heme Propionates in Coproheme Decarboxylase (HemQ)

Autor: Gudrun S. Lukat-Rodgers, Bennett R. Streit, George H. Gauss, Kenton R. Rodgers, Krista A. Shisler, Arianna I. Celis, John W. Peters, Garrett C. Moraski, Jennifer L. DuBois

Publikováno v: Journal of the American Chemical Society. 139:1900-1911

Coproheme decarboxylase catalyzes two sequential oxidative decarboxylations with H2O2 as the oxidant, coproheme III as substrate and cofactor, and heme b as the product. Each reaction breaks a C-C bond and results in net loss of hydride, via steps th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01e09b5196c8627155c54d69c336ffe5
https://doi.org/10.1021/jacs.6b11324

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The Crystal Structure of Six-transmembrane Epithelial Antigen of the Prostate 4 (Steap4), a Ferri/Cuprireductase, Suggests a Novel Interdomain Flavin-binding Site

Autor: Mark D. Fleming, C. Martin Lawrence, George H. Gauss, Mark D. Kleven, Anoop K. Sendamarai

Publikováno v: Journal of Biological Chemistry. 288:20668-20682

Steap4 is a cell surface metalloreductase linked to obesity-associated insulin resistance. Initial characterization of its cell surface metalloreductase activity has been reported, but thorough biochemical characterization of this activity is lacking

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::517ec017ce5909e2a58cc170ac93d3a4
https://doi.org/10.1074/jbc.m113.479154

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Substitution of a conserved catalytic dyad into 2-KPCC causes loss of carboxylation activity

Autor: Florence Mus, Gregory A. Prussia, George H. Gauss, John W. Peters, Jennifer L. DuBois, Leah Conner

Publikováno v: FEBS letters. 590(17)

The characteristic His-Glu catalytic dyad of the disulfide oxidoreductase (DSOR) family of enzymes is replaced in 2-Ketopropyl Coenzyme M Oxidoreductase/Carboxylase (2-KPCC) by the residues Phe-His. 2-KPCC is the only known carboxylating member of th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66ffd55a3bc6ac0581adb367ff392261
https://pubmed.ncbi.nlm.nih.gov/27447465

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Characterization of the Bacteroides fragilis bfr Gene Product Identifies a Bacterial DPS-Like Protein and Suggests Evolutionary Links in the Ferritin Superfamily

Autor: Michael A. Reott, Trevor Douglas, Edson R. Rocha, Mark J. Young, George H. Gauss, C J Smith, C.M. Lawrence

Publikováno v: Journal of Bacteriology. 194:15-27

A factor contributing to the pathogenicity of Bacteroides fragilis, the most common anaerobic species isolated from clinical infections, is the bacterium's extreme aerotolerance, which allows survival in oxygenated tissues prior to anaerobic abscess

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5ea95a647ffaa17f6f0a0cc38ef5fec
https://doi.org/10.1128/jb.05260-11

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Rotations of the 2B Sub-domain of E. coli UvrD Helicase/Translocase Coupled to Nucleotide and DNA Binding

Autor: Nasib K. Maluf, Anita Niedziela-Majka, Timothy M. Lohman, George H. Gauss, Haifeng Jia, Sergey Korolev, Gabriel Waksman, Taekjip Ha, Sua Myong

Publikováno v: Journal of Molecular Biology. 411:633-648

E. coli UvrD is a superfamily 1 (SF1) DNA helicase and single stranded (ss) DNA translocase that functions in DNA repair, plasmid replication and as an anti-recombinase by removing RecA protein from ssDNA. UvrD couples ATP binding and hydrolysis to u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a79b3029aba2e5b40924e731b03c962b
https://doi.org/10.1016/j.jmb.2011.06.019

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Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula

Autor: Corey J. Fugate, George H. Gauss, Danny Hicks, Matthew C. Posewitz, Oleg A. Zadvornyy, Eric S. Boyd, Jacob H. Artz, Spencer N. White, John W. Peters

Publikováno v: Frontiers in Bioengineering and Biotechnology, Vol 3 (2015)
Frontiers in Bioengineering and Biotechnology

Mercuric ion reductase (MerA), a mercury detoxification enzyme, has been tuned by evolution to have high specificity for mercuric ions (Hg2+) and to catalyze their reduction to a more volatile, less toxic elemental form. Here, we present a biochemica

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Structure of the DPS-Like Protein from Sulfolobus solfataricus Reveals a Bacterioferritin-Like Dimetal Binding Site within a DPS-Like Dodecameric Assembly

Autor: Blake Wiedenheft, Trevor Douglas, C.M. Lawrence, Philippe Benas, Mark J. Young, George H. Gauss

Publikováno v: Biochemistry. 45:10815-10827

Oxidative stress, in which reactive oxygen species (ROS1) react indiscriminately with DNA, proteins and lipids, is a universal phenomenon experienced by organisms in all domains of life. Cumulative damage from ROS is now thought to contribute to nume

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::551b8c43aee3f6088a97415e96d00ff5
https://doi.org/10.1021/bi060782u

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Structure of D-63 from Sulfolobus Spindle-Shaped Virus 1: Surface Properties of the Dimeric Four-Helix Bundle Suggest an Adaptor Protein Function

Autor: Mark J. Young, Daniel Kümmel, Paul Kraft, George H. Gauss, C. Martin Lawrence, Blake Wiedenheft, Andrea Oeckinghaus

Publikováno v: Journal of Virology. 78:7438-7442

Sulfolobus spindle-shaped virus 1 (SSV1) and its fusellovirus homologues can be found in many acidic (pH ≤ 4.0) hot springs (≥70°C) around the world. SSV1 contains a 15.5-kb double-stranded DNA genome that encodes 34 proteins with greater than 5

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8da8f843f18b083376eed6215c674462
https://doi.org/10.1128/jvi.78.14.7438-7442.2004

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The 2B domain of the Escherichia coli Rep protein is not required for DNA helicase activity

Autor: Sergey Korolev, Timothy M. Lohman, Wei Cheng, Gabriel Waksman, George H. Gauss, Katherine M. Brendza

Publikováno v: Proceedings of the National Academy of Sciences. 99:16006-16011

The Escherichia coli Rep protein is a 3′ to 5′ SF1 DNA helicase required for replication of bacteriophage φX174 in E. coli , and is structurally homologous to the E. coli UvrD helicase and the Bacillus stearothermophilus PcrA helicase. Previous

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb80994471d23cfe00d91dfd10795b87
https://doi.org/10.1073/pnas.242479399

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