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James Hennessy

Researcher at Australian National University

Publications -  20
Citations -  254

James Hennessy is an academic researcher from Australian National University. The author has contributed to research in topics: Catalysis & Cell-free protein synthesis. The author has an hindex of 7, co-authored 20 publications receiving 204 citations.

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Membranes from academia to industry

TL;DR: The perks and pitfalls of membrane research and development are talked about, and how activities at the new Barrer Centre might lead to next-generation separation technologies.
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Clostridium carboxidivorans strain P7T recombinant formate dehydrogenase catalyzes reduction of CO(2) to formate.

TL;DR: Recombinant formate dehydrogenase from the acetogen Clostridium carboxidivorans strain P7T, expressed in Escherichia coli, shows particular activity towards NADH-dependent carbon dioxide reduction to formate due to the relative binding affinities of the substrates and products.
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ATP Recycling with Cell Lysate for Enzyme-Catalyzed Chemical Synthesis, Protein Expression and PCR.

TL;DR: In this paper, the utility of this ATP recycling strategy in enzyme-catalyzed chemical synthesis is illustrated through the conversion of uridine to UMP by the lysate from recombinant overexpression of URINE with the E. coli.
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Cofactor promiscuity among F 420 -dependent reductases enables them to catalyse both oxidation and reduction of the same substrate

TL;DR: This work reports that three FDRs from Mycobacterium smegmatis also exhibit a different catalytic function towards some aflatoxins through the use of a different cofactor, the first example of an enzyme showing promiscuity for its cofactor leading to divergence of function against the same substrate.
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Incorporation of chlorinated analogues of aliphatic amino acids during cell-free protein synthesis

TL;DR: 3-Chloro-Abu and 4-chloro-Nva are biosynthetically incorporated into E. coli peptidyl-Pro cis-trans isomerase B, as substitutes for Val and Leu, respectively, and substituted protein is catalytically active.