James W.B. Moir

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Silver nanoparticles (AgNP) confined within porous starch have been prepared in a simple, green and efficient manner, utilising the nanoporous structure of predominantly mesoporous starch (MS) to act as nanoparticle stabiliser, support and reducing surface. MS/AgNP materials present high surface areas (S(BET) > 150 m(2) g(-1)) and mesopore volumes (V(meso)(More)
Members of the Neisseria genus typically display the ability to carry out denitrification of nitrite to nitrous oxide as an alternative to oxygen respiration when oxygen is depleted. The key enzymes nitrite and nitric oxide reductase are found across the Neisseria genus. Within Neisseria meningitidis, however, a number of research groups have found that a(More)
Neisseria meningitidis is a pathogenic bacterium responsible for meningitis. The mechanisms underlying the control of Na+ transmembrane movement, presumably important to pathogenicity, have been barely addressed. To elucidate the function of the components of the Na+ transport system in N. meningitidis, an open reading frame from the genome of this(More)
Naturally occurring oxygen tolerant NiFe membrane bound hydrogenases have a conserved catalytic bias towards hydrogen oxidation which limits their technological value. We present an Escherichia coli Hyd-1 amino acid exchange that apparently causes the catalytic rate of H2 production to double but does not impact the O2 tolerance.
Biology offers a source of inspiration for the discovery of highly active, precious-metal-free molecular H2 production (proton reduction) catalysts, because many microbes have evolved to produce hydrogen from protons and electrons (2H + 2e H2) using enzymes known as hydrogenases. Most nickel-iron hydrogenases, enzymes containing a NiFe bimetallic active(More)
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