Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803.
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Crystal structure of the catalytic subunit of magnesium chelatasePhotosynthetic capacity, nutrient status, and growth of maize (Zea mays L.) upon MgSO4 leaf-applicationTetrapyrrole Metabolism in Arabidopsis thaliana.Nanomechanical and Thermophoretic Analyses of the Nucleotide-Dependent Interactions between the AAA(+) Subunits of Magnesium Chelatase.Cyanobacteria metal interactions: requirements, toxicity, and ecological implications.Making the connections--the crucial role of metabolite transporters at the interface between chloroplast and cytosol.Direct Mg(2+) binding activates adenylate kinase from Escherichia coli.Factors controlling the reactivity of divalent metal ions towards pheophytin aStructure of the cyanobacterial Magnesium Chelatase H subunit determined by single particle reconstruction and small-angle X-ray scattering.Structural and functional consequences of removing the N-terminal domain from the magnesium chelatase ChlH subunit of Thermosynechococcus elongatus.A BchD (magnesium chelatase) mutant of rhodobacter sphaeroides synthesizes zinc bacteriochlorophyll through novel zinc-containing intermediates.Conserved residues in Ycf54 are required for protochlorophyllide formation in Synechocystis sp. PCC 6803.The catalytic power of magnesium chelatase: a benchmark for the AAA(+) ATPases.Catalytic turnover triggers exchange of subunits of the magnesium chelatase AAA+ motor unit.The allosteric role of the AAA+ domain of ChlD protein from the magnesium chelatase of synechocystis species PCC 6803.Characterization of the magnesium chelatase from Thermosynechococcus elongatus.Kinetic analyses of the magnesium chelatase provide insights into the mechanism, structure, and formation of the complex.Fine tuning of copper(II)-chlorophyll interactions in organic media. Metalation versus oxidation of the macrocycle.Characterization of three homologs of the large subunit of the magnesium chelatase from Chlorobaculum tepidum and interaction with the magnesium protoporphyrin IX methyltransferase.
P2860
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P2860
Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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@zh-hans
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name
Magnesium-dependent ATPase act ...... rom Synechocystis sp. PCC6803.
@en
Magnesium-dependent ATPase act ...... rom Synechocystis sp. PCC6803.
@nl
type
label
Magnesium-dependent ATPase act ...... rom Synechocystis sp. PCC6803.
@en
Magnesium-dependent ATPase act ...... rom Synechocystis sp. PCC6803.
@nl
prefLabel
Magnesium-dependent ATPase act ...... rom Synechocystis sp. PCC6803.
@en
Magnesium-dependent ATPase act ...... rom Synechocystis sp. PCC6803.
@nl
P2860
P356
P1476
Magnesium-dependent ATPase act ...... rom Synechocystis sp. PCC6803.
@en
P2093
C Neil Hunter
P2860
P304
26893-26899
P356
10.1074/JBC.M400958200
P407
P577
2004-03-29T00:00:00Z