M
Michael W. W. Adams
Researcher at University of Georgia
Publications - 474
Citations - 26318
Michael W. W. Adams is an academic researcher from University of Georgia. The author has contributed to research in topics: Pyrococcus furiosus & Ferredoxin. The author has an hindex of 83, co-authored 473 publications receiving 24425 citations. Previous affiliations of Michael W. W. Adams include Oak Ridge National Laboratory & California Institute of Technology.
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Journal ArticleDOI
The structure and mechanism of iron-hydrogenases
TL;DR: Mechanisms of H2 activation and electron transfer are proposed to explain the effects of CO binding and the ability of one of the hydrogenases to preferentially catalyze H2 oxidation and H2 production.
Journal ArticleDOI
High-fidelity amplification using a thermostable DNA polymerase isolated from Pyrococcus furiosus
Kelly S. Lundberg,Daniel D. Abrahms Apartment C Shoemaker,Michael W. W. Adams,Jay M. Short,Joseph A. Sorge,Eric J. Mathur +5 more
TL;DR: These studies demonstrate that the error rate per nucleotide induced in the 182 known detectable sites of the lacI gene was 1.6 x 10(-6) for Pfu DNA polymerase, a greater than tenfold improvement over the 2.0 x 10 (-5) error rate for Taq DNA polymerases.
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Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)
Greg L. Hura,Angeli Lal Menon,Michal Hammel,Robert P. Rambo,Farris L. Poole,Susan E. Tsutakawa,Francis E. Jenney,Francis E. Jenney,Scott Classen,Kenneth A. Frankel,Robert C. Hopkins,Sung-Jae Yang,Joseph W. Scott,Bret D. Dillard,Michael W. W. Adams,John A. Tainer +15 more
TL;DR: The SAXS pipeline combines automated sample handling of microliter volumes, temperature and anaerobic control, rapid data collection and data analysis, and couples structural analysis with automated archiving to create an efficient pipeline enabling high-throughput analysis of protein structure in solution with small angle X-ray scattering.
Journal ArticleDOI
Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
TL;DR: The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus, a hyperthermophilic archaeon that grows optimally at 100 degrees C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal form averaging.
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The Iron-Hydrogenase of Thermotoga maritima Utilizes Ferredoxin and NADH Synergistically: a New Perspective on Anaerobic Hydrogen Production
TL;DR: The discovery of the bifurcating hydrogenase gives a new perspective on the understanding of the bioenergetics and mechanism of H(2) production and of anaerobic metabolism in general.