1-11 of 11
David J. Lowe
Close
Save search
Follow your search
Access your saved searches in your account
Would you like to receive an alert when new items match your search?
Close Modal
Sort by
Articles

Evidence for a dynamic role for homocitrate during nitrogen fixation: the effect of substitution at the α-Lys 426 position in MoFe-protein of Azotobacter vinelandii

Available to Purchase
Marcus C. Durrant, Amanda Francis, David J. Lowe, William E. Newton, Karl Fisher
Journal: Biochemical Journal
Biochem J (2006) 397 (2): 261–270.
https://doi.org/10.1042/BJ20060102
Published: 28 June 2006
View articletitled, Evidence for a dynamic role for homocitrate during nitrogen fixation: the effect of substitution at the α-Lys 426 position in MoFe-protein of Azotobacter vinelandii
Open the PDF for Evidence for a dynamic role for homocitrate during nitrogen fixation: the effect of substitution at the α-Lys 426 position in MoFe-protein of Azotobacter vinelandii in another window
Articles

Mn 2+ -adenosine nucleotide complexes in the presence of the nitrogenase iron-protein: detection of conformational rearrangements directly at the nucleotide binding site by EPR and 2D-ESEEM (two-dimensional electron spin-echo envelope modulation spectroscopy)

Available to Purchase
Jan Petersen, Christof Gessner, Karl Fisher, Claire J. Mitchell, David J. Lowe, Wolfgang Lubitz
Journal: Biochemical Journal
Biochem J (2005) 391 (3): 527–539.
https://doi.org/10.1042/BJ20050226
Published: 25 October 2005
View articletitled, Mn 2+ -adenosine nucleotide complexes in the presence of the nitrogenase iron-protein: detection of conformational rearrangements directly at the nucleotide binding site by EPR and 2D-ESEEM (two-dimensional electron spin-echo envelope modulation spectroscopy)
Open the PDF for Mn 2+ -adenosine nucleotide complexes in the presence of the nitrogenase iron-protein: detection of conformational rearrangements directly at the nucleotide binding site by EPR and 2D-ESEEM (two-dimensional electron spin-echo envelope modulation spectroscopy) in another window
Includes: Supplementary data
Articles

Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres

Available to Purchase
Benjamin L. J. GODBER, Guenter SCHWARZ, Ralf R. MENDEL, David J. LOWE, Robert C. BRAY, Robert EISENTHAL, Roger HARRISON
Journal: Biochemical Journal
Biochem J (2005) 388 (2): 501–508.
https://doi.org/10.1042/BJ20041984
Published: 24 May 2005
View articletitled, Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres
Open the PDF for Molecular characterization of human xanthine oxidoreductase: the enzyme is grossly deficient in molybdenum and substantially deficient in iron-sulphur centres in another window
Articles

Mo(V) co-ordination in the periplasmic nitrate reductase from Paracoccus pantotrophus probed by electron nuclear double resonance (ENDOR) spectroscopy

Available to Purchase
Clive S. BUTLER, Shirley A. FAIRHURST, Stuart J. FERGUSON, Andrew J. THOMSON, Ben C. BERKS, David J. RICHARDSON, David J. LOWE
Journal: Biochemical Journal
Biochem J (2002) 363 (3): 817–823.
https://doi.org/10.1042/bj3630817
Published: 24 April 2002
View articletitled, Mo(V) co-ordination in the periplasmic nitrate reductase from Paracoccus pantotrophus probed by electron nuclear double resonance (ENDOR) spectroscopy
Open the PDF for Mo(V) co-ordination in the periplasmic nitrate reductase from Paracoccus pantotrophus probed by electron nuclear double resonance (ENDOR) spectroscopy in another window
Articles

Expression of Drosophila melanogaster xanthine dehydrogenase in Aspergillus nidulans and some properties of the recombinant enzyme

Available to Purchase
Benjamin ADAMS, David J. LOWE, Andrew T. SMITH, Claudio SCAZZOCCHIO, Stephane DEMAIS, Robert C. BRAY
Journal: Biochemical Journal
Biochem J (2002) 362 (2): 223–229.
https://doi.org/10.1042/bj3620223
Published: 22 February 2002
View articletitled, Expression of Drosophila melanogaster xanthine dehydrogenase in Aspergillus nidulans and some properties of the recombinant enzyme
Open the PDF for Expression of Drosophila melanogaster xanthine dehydrogenase in Aspergillus nidulans and some properties of the recombinant enzyme in another window
Articles

Reaction of variant sperm-whale myoglobins with hydrogen peroxide: the effects of mutating a histidine residue in the haem distal pocket

Available to Purchase
Thomas BRITTAIN, Adam R. BAKER, Clive S. BUTLER, Richard H. LITTLE, David J. LOWE, Colin GREENWOOD, Nicholas J. WATMOUGH
Journal: Biochemical Journal
Biochem J (1997) 326 (1): 109–115.
https://doi.org/10.1042/bj3260109
Published: 15 August 1997
View articletitled, Reaction of variant sperm-whale myoglobins with hydrogen peroxide: the effects of mutating a histidine residue in the haem distal pocket
Open the PDF for Reaction of variant sperm-whale myoglobins with hydrogen peroxide: the effects of mutating a histidine residue in the haem distal pocket in another window
Articles

pH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans

Available to Purchase
Zelda. H. L ABRAHAM, Barry. E SMITH, Barry. D HOWES, David. J LOWE, Robert. R EADY
Journal: Biochemical Journal
Biochem J (1997) 324 (2): 511–516.
https://doi.org/10.1042/bj3240511
Published: 01 June 1997
View articletitled, pH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans
Open the PDF for pH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans in another window
Articles

Distribution of reducing equivalents on xanthine oxidase molecules and the rates of the intramolecular electron-transfer reactions

Available to Purchase
Robert C. Bray, David J. Lowe, Michael J. Barber
Journal: Biochemical Journal
Biochem J (1974) 141 (1): 309–311.
https://doi.org/10.1042/bj1410309
Published: 01 July 1974
View articletitled, Distribution of reducing equivalents on xanthine oxidase molecules and the rates of the intramolecular electron-transfer reactions
Open the PDF for Distribution of reducing equivalents on xanthine oxidase molecules and the rates of the intramolecular electron-transfer reactions in another window
Articles

The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis

Available to Purchase
E. Martin Fielden, Peter B. Roberts, Robert C. Bray, David J. Lowe, Gillian N. Mautner, Giuseppe Rotilio, Lilia Calabrese
Journal: Biochemical Journal
Biochem J (1974) 139 (1): 49–60.
https://doi.org/10.1042/bj1390049
Published: 01 April 1974
View articletitled, The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis
Open the PDF for The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis in another window
Articles

Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae

Available to Purchase
Barry E. Smith, David J. Lowe, Robert C. Bray
Journal: Biochemical Journal
Biochem J (1973) 135 (2): 331–341.
https://doi.org/10.1042/bj1350331
Published: 01 October 1973
View articletitled, Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae
Open the PDF for Studies by electron paramagnetic resonance on the catalytic mechanism of nitrogenase of Klebsiella pneumoniae in another window
Articles

Spin–spin interaction between molybdenum and one of the iron–sulphur systems of xanthine oxidase and its relevance to the enzymic mechanism

Available to Purchase
David J. Lowe, Ruth M. Lynden-Bell, Robert C. Bray
Journal: Biochemical Journal
Biochem J (1972) 130 (1): 239–249.
https://doi.org/10.1042/bj1300239
Published: 01 November 1972
View articletitled, Spin–spin interaction between molybdenum and one of the iron–sulphur systems of xanthine oxidase and its relevance to the enzymic mechanism
Open the PDF for Spin–spin interaction between molybdenum and one of the iron–sulphur systems of xanthine oxidase and its relevance to the enzymic mechanism in another window