Structural and mechanistic basis of porphyrin metallation by ferrochelatase
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The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase.Chelatases: distort to select?Structure of the Mg-chelatase cofactor GUN4 reveals a novel hand-shaped fold for porphyrin binding.Substrate interactions with human ferrochelataseAltered Orientation of Active Site Residues in Variants of Human Ferrochelatase. Evidence for a Hydrogen Bond Network Involved in Catalysis †A pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.Porphyrin Binding and Distortion and Substrate Specificity in the Ferrochelatase Reaction: The Role of Active Site ResiduesEvolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerizationOccurrence, conformational features and amino acid propensities for the pi-helixSubstitution of murine ferrochelatase glutamate-287 with glutamine or alanine leads to porphyrin substrate-bound variantsThe heme biosynthetic pathway of the obligate Wolbachia endosymbiont of Brugia malayi as a potential anti-filarial drug targetPorphyrin-substrate binding to murine ferrochelatase: effect on the thermal stability of the enzymeProbing the active site loop motif of murine ferrochelatase by random mutagenesisQuantum chemical geometry optimizations in proteins using crystallographic raw data.Resonance Raman and vibrational mode analysis used to predict ligand geometry for docking simulations of a water soluble porphyrin and tubulin.A high-throughput screen for porphyrin metal chelatases: application to the directed evolution of ferrochelatases for metalloporphyrin biosynthesis.The enigma of cobalamin (Vitamin B12) biosynthesis in Porphyromonas gingivalis. Identification and characterization of a functional corrin pathway.Discovery and Characterization of HemQ: an essential heme biosynthetic pathway component.Nickel(II) chelatase variants directly evolved from murine ferrochelatase: porphyrin distortion and kinetic mechanism.Resonance Raman Spectroscopic Examination of Ferrochelatase-induced Porphyrin Distortion.FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYSIdentification and characterization of solvent-filled channels in human ferrochelatase.Direct measurement of metal ion chelation in the active site of human ferrochelatase.Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.In vivo and in vitro studies of Bacillus subtilis ferrochelatase mutants suggest substrate channeling in the heme biosynthesis pathway.Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.Modulation of inhibition of ferrochelatase by N-methylprotoporphyrin.The coproporphyrin ferrochelatase of Staphylococcus aureus: mechanistic insights into a regulatory iron-binding site.Prediction of the interaction of metallic moieties with proteins: An update for protein-ligand docking techniques.
P2860
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P2860
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
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2000 nî lūn-bûn
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2000 թուականի Մարտին հրատարակուած գիտական յօդուած
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2000年の論文
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2000年論文
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2000年論文
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name
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@ast
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@en
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
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type
label
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@ast
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@en
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@nl
prefLabel
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@ast
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@en
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@nl
P2093
P356
P1476
Structural and mechanistic basis of porphyrin metallation by ferrochelatase
@en
P2093
P304
P356
10.1006/JMBI.2000.3569
P407
P577
2000-03-17T00:00:00Z