Magnesium chelatase from Rhodobacter sphaeroides: initial characterization of the enzyme using purified subunits and evidence for a BchI-BchD complex.
about
Purification and kinetic characterization of the magnesium protoporphyrin IX methyltransferase from Synechocystis PCC6803The CoxD protein of Oligotropha carboxidovorans is a predicted AAA+ ATPase chaperone involved in the biogenesis of the CO dehydrogenase [CuSMoO2] cluster.Porphyrin Binding to Gun4 Protein, Facilitated by a Flexible Loop, Controls Metabolite Flow through the Chlorophyll Biosynthetic Pathway.Three semidominant barley mutants with single amino acid substitutions in the smallest magnesium chelatase subunit form defective AAA+ hexamers.The CoxD protein, a novel AAA+ ATPase involved in metal cluster assembly: hydrolysis of nucleotide-triphosphates and oligomerization.Nanomechanical and Thermophoretic Analyses of the Nucleotide-Dependent Interactions between the AAA(+) Subunits of Magnesium Chelatase.Modulation of chlorophyll biosynthesis by water stress in rice seedlings during chloroplast biogenesis.ATPase activity associated with the magnesium chelatase H-subunit of the chlorophyll biosynthetic pathway is an artefact.Structure 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.Transient kinetics of the reaction catalysed by magnesium protoporphyrin IX methyltransferase.ATPase activity associated with the magnesium-protoporphyrin IX chelatase enzyme of Synechocystis PCC6803: evidence for ATP hydrolysis during Mg2+ insertion, and the MgATP-dependent interaction of the ChlI and ChlD subunits.Modification of cysteine residues in the ChlI and ChlH subunits of magnesium chelatase results in enzyme inactivation.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.Magnesium-dependent ATPase activity and cooperativity of magnesium chelatase from Synechocystis sp. PCC6803.Substrate-binding model of the chlorophyll biosynthetic magnesium chelatase BchH subunit.Superoxide generation by chlorophyllide a reductase of Rhodobacter sphaeroides.Recessiveness and dominance in barley mutants deficient in Mg-chelatase subunit D, an AAA protein involved in chlorophyll biosynthesis.Phosphorylation of GENOMES UNCOUPLED 4 Alters Stimulation of Mg Chelatase Activity in Angiosperms.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 chelatase from Rhodobacter sphaeroides: initial characterization of the enzyme using purified subunits and evidence for a BchI-BchD complex.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Magnesium chelatase from Rhodo ...... dence for a BchI-BchD complex.
@en
Magnesium chelatase from Rhodo ...... dence for a BchI-BchD complex.
@nl
type
label
Magnesium chelatase from Rhodo ...... dence for a BchI-BchD complex.
@en
Magnesium chelatase from Rhodo ...... dence for a BchI-BchD complex.
@nl
prefLabel
Magnesium chelatase from Rhodo ...... dence for a BchI-BchD complex.
@en
Magnesium chelatase from Rhodo ...... dence for a BchI-BchD complex.
@nl
P2860
P1433
P1476
Magnesium chelatase from Rhodo ...... idence for a BchI-BchD complex
@en
P2093
P2860
P304
P356
10.1042/0264-6021:3370243
10.1042/BJ3370243
P407
P478
337 ( Pt 2)
P577
1999-01-01T00:00:00Z