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Your search keyword '"Boulanger, Martin J."' showing total 3 results
Start Over Author "Boulanger, Martin J." Journal biochemistry
3 results on '"Boulanger, Martin J."'

1. Alternate substrate binding modes to two mutant (D98N and H255N) forms of nitrite reductase from Alcaligenes faecalis S-6: structural model of a transient catalytic intermediate

Author

Boulanger, Martin J. and Murphy, Michael E. P.

Subjects
Biochemistry -- Research, Gene mutations -- Physiological aspects, Bacteria -- Genetic aspects, Nitrites -- Genetic aspects, Oxidation-reduction reaction -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the mutant forms of the nitrite reductase from Alcaligenes faecalis S-6. The nitrite soaked high-resolution oxidised and reduced crystal structures of these mutants have been investigated and the results are presented.

Published
2001

2. Identification and characterization of binding sites on s100A7, a participant in cancer and inflammation pathways

Author

Leon, Rafael, Murray, Jill I., Cragg, Gina, Farnell, Benjamin, West, Nathan R., Pace, Tamara C.S., Watson, Peter H., Bohne, Cornelia, Boulanger, Martin J., and Hof, Fraser

Subjects
Gene mutations -- Analysis, Hydrophobic effect -- Analysis, Naphthalene -- Structure, Naphthalene -- Chemical properties, Protein binding -- Analysis, Biological sciences, Chemistry
Abstract

Several studies are conducted to explain the identification, as well as the characterization of the various binding sites on s100A7 (psoriasin), a member of the family of cancer signaling proteins. The protein is shown to play an extremely significant role as a therapeutic target for inflammation, as well as cancer.

Published
2009

3. Reconstitution of the type-1 active site of the H145G/A variants of nitrite reductase by ligand insertion

Author

Wijma, Hein J., Boulanger, Martin J., Molon, Annamaria, Fittipaldi, Maria, Huber, Martina, Murphy, Michael E.P., Verbeet, Martin Ph., and Canters, Gerard W.

Subjects
Binding sites (Biochemistry) -- Analysis, Oxidation-reduction reaction -- Physiological aspects, Enzymes -- Structure-activity relationship, Biological sciences, Chemistry
Abstract

Results indicate that exogenous ligands can bind to the oxidized type-1 site to restore the site's normal spectroscopic properties, while the reduced type-1 site does not bind exogenous ligands. Furthermore, the rates of electron transfer to the oxidized type-1 sites in the nitrite reductase variants are similar to native types, in the presence of exogenous ligands.

Published
2003

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