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The molecular basis of phosphite and hypophosphite recognition by ABC-transporters
Inorganic phosphate is the major bioavailable form of the essential nutrient phosphorus. However, the concentration of phosphate in most natural habitats is low enough to limit microbial growth.Expand
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Advances in Gas Phase Ion Chemistry
Flow tube studies of small isometric ions, Murray J. McEwan anion-molecule experiments - reactive intermediates and mechanistic organic chemistry, Joseph J. Grabowski thermochemical measurements byExpand
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Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo–designed heme protein
Protein transport across the cytoplasmic membrane of bacterial cells is mediated by either the general secretion (Sec) system or the twin-arginine translocase (Tat). The Tat machinery exports foldedExpand
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The Allosteric Role of the AAA+ Domain of ChlD Protein from the Magnesium Chelatase of Synechocystis Species PCC 6803*
Background: Magnesium chelatase catalyzes the first essential step in chlorophyll biosynthesis. Results: Mutations in the AAA+ domain of the magnesium chelatase ChlD subunit reduce but do not abolishExpand
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Synthesis and Evaluation of Anticancer Natural Product Analogues Based on Angelmarin: Targeting the Tolerance towards Nutrient Deprivation
Inspired by nature: Angelmarin is an anticancer natural product with potent antiausterity activity, that is, selective cytotoxicity towards nutrient-deprived, resistant cancer cells. ThroughExpand
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Characterization of the magnesium chelatase from Thermosynechococcus elongatus.
The first committed step in chlorophyll biosynthesis is catalysed by magnesium chelatase (E.C. 6.6.1.1), which uses the free energy of ATP hydrolysis to insert an Mg(2+) ion into the ring ofExpand
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Nonequilibrium isotope exchange reveals a catalytically significant enzyme-phosphate complex in the ATP hydrolysis pathway of the AAA(+) ATPase magnesium chelatase.
Magnesium chelatase is an AAA(+) ATPase that catalyzes the first committed step in chlorophyll biosynthesis. Using nonequilibrium isotope exchange, we show that the ATP hydrolysis reaction proceedsExpand
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Nanomechanical and Thermophoretic Analyses of the Nucleotide-Dependent Interactions between the AAA+ Subunits of Magnesium Chelatase
In chlorophyll biosynthesis, the magnesium chelatase enzyme complex catalyzes the insertion of a Mg2+ ion into protoporphyrin IX. Prior to this event, two of the three subunits, the AAA+ proteinsExpand
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Porphyrin Binding to Gun4 Protein, Facilitated by a Flexible Loop, Controls Metabolite Flow through the Chlorophyll Biosynthetic Pathway*
Background: The Gun4 protein stimulates activity of magnesium chelatase, and it is important for chlorophyll biosynthesis. Results: Mechanism of porphyrin binding by Gun4 was proposed, and a Gun4Expand
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The ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase
Magnesium chelatase initiates chlorophyll biosynthesis, catalysing the MgATP2−-dependent insertion of a Mg2+ ion into protoporphyrin IX. The catalytic core of this large enzyme complex consists ofExpand
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