W
William W. Metcalf
Researcher at University of Illinois at Urbana–Champaign
Publications - 167
Citations - 11242
William W. Metcalf is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Methanosarcina acetivorans & Methanosarcina. The author has an hindex of 57, co-authored 156 publications receiving 9737 citations. Previous affiliations of William W. Metcalf include Purdue University & Howard Hughes Medical Institute.
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Development of a Markerless Genetic Exchange Method for Methanosarcina acetivorans C2A and Its Use in Construction of New Genetic Tools for Methanogenic Archaea
TL;DR: A new genetic technique for constructing mutants of Methanosarcina acetivorans C2A by using hpt as a counterselectable marker was developed and the markerless exchange method was used to recombine a series of uidA reporter gene fusions into the M. acetIVorans proC locus.
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Diversity and abundance of phosphonate biosynthetic genes in nature
Xiaomin Yu,James R. Doroghazi,Sarath Chandra Janga,Jun Kai Zhang,Benjamin T. Circello,Benjamin M. Griffin,David P. Labeda,William W. Metcalf +7 more
TL;DR: The data presented here show that the ability to synthesize diverse phosphonates is both widespread and relatively common among microbes, supporting the idea that these molecules play a significant role in the biology of producing organisms and suggesting that the role of phosphonate molecules in the biosphere may be more important than is often recognized.
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A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase
Kechao Yang,William W. Metcalf +1 more
TL;DR: Surprisingly, BAP catalyzes the oxidation of Pt to phosphate and molecular H2 and is a unique Pt-dependent, H2-evolving hydrogenase, which is unprecedented in both P and H biochemistry.
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Mutational analysis of an Escherichia coli fourteen-gene operon for phosphonate degradation, using TnphoA' elements.
TL;DR: The results indicate that the PhnC-to-phnP gene cluster is an operon of 14 genes, and the phnC promoter is the sole psi promoter; three gene products probably constitute a binding protein-dependent Pn transporter; seven gene products are required for catalysis and are likely to constitute a membrane-associated carbon-phosphorus (C-P) lyase; and two gene products may be accessory proteins for the C-P lyase.