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- 2008
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Mark
Substrate-binding model of the chlorophyll biosynthetic magnesium chelatase BchH subunit.
(
- Contribution to journal › Article
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Mark
Porphyrin Binding and Distortion and Substrate Specificity in the Ferrochelatase Reaction: The Role of Active Site Residues.
(
- Contribution to journal › Article
- 2007
-
Mark
Comparing two microarray platforms for identifying mutated genes in barley (Hordeum vulgare L.)
(
- Contribution to journal › Article
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Mark
Rhodobacter capsulatus magnesium chelatase subunit BchH contains an oxygen sensitive iron-sulfur cluster
(
- Contribution to journal › Article
-
Mark
Ethical framework for previously collected biobank samples
(
- Contribution to journal › Letter
-
Mark
Amino acid residues His183 and Glu264 in Bacillus subtilis ferrochelatase direct and facilitate the insertion of metal ion into protoporphyrin IX
(
- Contribution to journal › Article
-
Mark
A new method for isolating physiologically active Mg-protoporphyrin
(
- Contribution to journal › Article
- 2006
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Mark
Crosstalk between metal ions in Bacillus subtilis ferrochelatase
(
- Contribution to journal › Article
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Mark
Chelatases: distort to select?
(
- Contribution to journal › Debate/Note/Editorial
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Mark
ATPase activity associated with the magnesium chelatase H-subunit of the chlorophyll biosynthetic pathway is an artefact
(
- Contribution to journal › Article