Zobrazeno 1 - 10
of 17
pro vyhledávání: '"James D. Gwyer"'
Autor:
Vladimir Popov, Thomas G. Lowe, Tamara V. Tikhonova, Julea N. Butt, Sophie J. Marritt, James D. Gwyer, Myles R. Cheesman, Rose-Marie A. S. Doyle
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 18:655-667
The multiheme cytochromes from Thioalkalivibrio nitratireducens (TvNiR) and Escherichia coli (EcNrfA) reduce nitrite to ammonium. Both enzymes contain His/His-ligated hemes to deliver electrons to their active sites, where a Lys-ligated heme has a di
Publikováno v:
Analytical Chemistry. 84:1070-1075
This paper demonstrates an integrated microfluidic system that performs a full blood count using impedance analysis. A microfluidic network design for red blood cell (RBC) lysis is presented, and the diffusive mixing processes are analyzed using expe
Autor:
Lars J. C. Jeuken, James K. R. Kendall, Phil Symonds, James D. Gwyer, Stephen D. Evans, Cees van Berkel, Benjamin R. G. Johnson, Guiseppi Imperato, Richard J. Bushby
Publikováno v:
ChemPhysChem. 11:2191-2198
Tethered bilayer lipid membranes (tBLM) are formed on 1) pure tether lipid triethyleneoxythiol cholesterol (EO(3)C) or on 2) mixed self-assembled monolayers (SAMs) of EO(3)C and 6-mercaptohexanol (6MH). While EO(3)C is required to form a tBLM with hi
Publikováno v:
Biophysical Journal. 91(10):3897-3906
Escherichia coli cytochrome c nitrite reductase (NrfA) catalyzes the six-electron reduction of nitrite to perform an important role in the biogeochemical cycling of nitrogen. Here we describe NrfA adsorption on single-crystal Au(111) electrodes as an
Publikováno v:
Biochemistry. 43:15086-15094
Cytochrome c nitrite reductase is a dimeric decaheme-containing enzyme that catalyzes the reduction of nitrite to ammonium. The contrasting effects of two inhibitors on the activity of this enzyme have been revealed, and defined, by protein film volt
Publikováno v:
Bioelectrochemistry. 63:43-47
Escherichia coli cytochrome c nitrite reductase is a homodimeric enzyme whose 10 heme centres range in reduction potential from ca. -30 to -320 mV. Protein film voltammetry (PFV) was performed to assess how the reactivity of the enzyme towards a numb
Autor:
Cees, van Berkel, James D, Gwyer, Steve, Deane, Nicolas G, Green, Nicolas, Green, Judith, Holloway, Veronica, Hollis, Hywel, Morgan
Publikováno v:
Lab on a chip. 11(7)
Counting the different subpopulations of cells in a fingerprick of human blood is important for a number of clinical point-of-care (PoC) applications. It is a challenge to demonstrate the integration of sample preparation and detection techniques in
Autor:
James D. Gwyer, Thomas A. Clarke, B. Burlat, Myles R. Cheesman, Susannah R. Poock, J. A. Cole, Andrew M. Hemmings, David J. Richardson, Julea N. Butt
Publikováno v:
CIÊNCIAVITAE
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The recent structural characterization of the NrfA from Escherichia coli provides a framework to rationalize the spectroscopic and functional properties of this enzyme. Analyses by EPR and magnetic CD spectroscopies have been complemented by protein-
Publikováno v:
Journal of the American Chemical Society. 127:14964-14965
Protein film voltammetry has been employed to define multiple catalytic consequences of proton coupled electron transfer (PCET) in a cytochrome c nitrite reductase. Current-potential profiles reflecting the steady-state rate of nitrite-limited reduct
Leukocyte analysis and differentiation using high speed microfluidic single cell impedance cytometry
Autor:
James D. Gwyer, Donna E. Davies, Christian H. Reccius, Hywel Morgan, David M. Pettigrew, Cees van Berkel, David Holmes, Judith A. Holloway
Publikováno v:
Lab on a Chip. 9:2881
Miniature high speed label-free cell analysis systems have yet to be developed, but have the potential to deliver fast, inexpensive and simple full blood cell analysis systems that could be used routinely in clinical practice. We demonstrate a microf