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Journal of Bacteriology|December 15, 2000
Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzymeG Butland, S Spiro, N J Watmough, et al.Ultrasound in Medicine & Biology|November 1, 1983
Local hyperthermia induced by focussed and overlapping ultrasonic fields--an in vivo demonstrationK Hynynen, D J Watmough, J R Mallard, et al.Ultrasound in Medicine & Biology|April 1, 1986
A new motor-driven surgical probe and its in vitro comparison with the Cavitron Ultrasonic Surgical AspiratorK K Chan, D J Watmough, D T Hope, et al.The British Journal of Radiology|December 1, 1996
Case report: tuberculosis of the parotid gland--diagnosis by CTS Bhargava, D J Watmough, F A Chisti, et al.Journal of Inorganic Biochemistry|April 1, 2009
Exploring the terminal region of the proton pathway in the bacterial nitric oxide reductaseUlrika Flock, Peter Lachmann, Joachim Reimann, et al.The Biochemical Journal|August 15, 1989
Measurement of the acyl-CoA intermediates of beta-oxidation by h.p.l.c. with on-line radiochemical and photodiode-array detection. Application to the study of [U-14C]hexadecanoate oxidation by intact rat liver mitochondriaN J Watmough, D M Turnbull, H S Sherratt, et al.The Biochemical Journal|June 1, 1994
Cytochrome bo from Escherichia coli: reaction of the oxidized enzyme with hydrogen peroxideN J Watmough, M R Cheesman, C Greenwood, et al.The Biochemical Journal|September 12, 2006
A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzymeFaye H Thorndycroft, Gareth Butland, David J Richardson, et al.The Biochemical Journal|August 15, 1990
Intermediates of peroxisomal beta-oxidation. A study of the fatty acyl-CoA esters which accumulate during peroxisomal beta-oxidation of [U-14C]hexadecanoateK Bartlett, R Hovik, S Eaton, et al.Biochemistry|July 18, 2001
Intramolecular electron transfer from c heme to d1 heme in bacterial cytochrome cd1 nitrite reductase occurs over the same distances at very different rates depending on the source of the enzymeK Kobayashi, A Koppenhöfer, S J Ferguson, et al.Pageof 12