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Eric S. Boyd
Researcher at Montana State University
Publications - 170
Citations - 7678
Eric S. Boyd is an academic researcher from Montana State University. The author has contributed to research in topics: Nitrogenase & Medicine. The author has an hindex of 46, co-authored 151 publications receiving 6188 citations. Previous affiliations of Eric S. Boyd include NASA Astrobiology Institute & University of Wisconsin-Madison.
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Engineering algae for biohydrogen and biofuel production
TL;DR: There is currently substantial interest in utilizing eukaryotic algae for the renewable production of several bioenergy carriers, including starches for alcohols, lipids for diesel fuel surrogates, and H2 for fuel cells.
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[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation
John W. Peters,Gerrit J. Schut,Eric S. Boyd,David W. Mulder,Eric M. Shepard,Joan B. Broderick,Paul W. King,Michael W. W. Adams +7 more
TL;DR: These mechanisms represent two independent solutions to the formation of complex bioinorganic active sites for catalyzing the simplest of chemical reactions, reversible hydrogen oxidation, and are arguably the most profound case of convergent evolution.
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Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG).
David W. Mulder,Eric S. Boyd,Ranjana Sarma,Rachel K. Lange,James A. Endrizzi,Joan B. Broderick,John W. Peters +6 more
TL;DR: In this article, the X-ray crystal structure of Chlamydomonas reinhardtii HydA was solved, revealing the stepwise manner by which the H-cluster is synthesized, and offering insight into how HydA might have evolved.
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The mercury resistance operon: from an origin in a geothermal environment to an efficient detoxification machine
Eric S. Boyd,Tamar Barkay +1 more
TL;DR: The data suggest that (i) mer has evolved from a simple system in geothermal environments to a widely distributed and more complex and efficient detoxification system, and (ii) merA is a suitable biomarker for examining the functional diversity of Hg detoxification and for predicting the composition of mer operons in natural environments.
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The membrane-associated methane monooxygenase (pMMO) and pMMO-NADH:quinone oxidoreductase complex from Methylococcus capsulatus bath
Dong W. Choi,Ryan C. Kunz,Eric S. Boyd,Jeremy D. Semrau,William E. Antholine,Jong-In Han,James A. Zahn,James A. Zahn,Jeffrey M. Boyd,Arlene de la Mora,Alan A. DiSpirito +10 more
TL;DR: It is demonstrated that copper not only regulates the metabolic switch between the two methane monooxygenases but also regulates the level of expression of the pMMO and the development of internal membranes.