Probing the active site loop motif of murine ferrochelatase by random mutagenesis (Q28590153)

Journal of Biological Chemistry

GOA release 2020-03-11

author name string

Zhen Shi

series ordinal

1

1 reference

31 January 2017

Gloria C. Ferreira

series ordinal

2

1 reference

31 January 2017

language of work or name

English

0 references

publication date

7 May 2004

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31 January 2017

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31 January 2017

279

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19

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31 January 2017

19977–19986

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31 January 2017

Structure and function of ferrochelatase.

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Ferrochelatase at the millennium: structures, mechanisms and [2Fe-2S] clusters

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Human ferrochelatase is an iron-sulfur protein.

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Identification of [2Fe-2S] clusters in microbial ferrochelatases

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Systematic analysis of molecular defects in the ferrochelatase gene from patients with erythropoietic protoporphyria

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Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis

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Structural and mechanistic basis of porphyrin metallation by ferrochelatase

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The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis

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Photosensitivity of a protoporphyrin-accumulating, light-sensitive mutant (visA) of Escherichia coli K-12

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Random sequence mutagenesis and resistance to 5-fluorouridine in human thymidylate synthases

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DNA sequencing with chain-terminating inhibitors

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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A continuous anaerobic fluorimetric assay for ferrochelatase by monitoring porphyrin disappearance

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Global analysis of protein activities using proteome chips

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Geno3D: automatic comparative molecular modelling of protein.

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VMD: visual molecular dynamics

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Site-directed mutagenesis of human ferrochelatase: identification of histidine-263 as a binding site for metal ions.

21 January 2018

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Human ferrochelatase: characterization of substrate-iron binding and proton-abstracting residues

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Occurrence, conformational features and amino acid propensities for the pi-helix

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Isolation and functional characterization of mutant ferrochelatases in Saccharomyces cerevisiae.

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Stabilization of a reaction intermediate as a catalytic device: definition of the functional role of the flexible loop in triosephosphate isomerase.

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Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism

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Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase

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Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mössbauer methods.

21 January 2018

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Unraveling the substrate-metal binding site of ferrochelatase: an X-ray absorption spectroscopic study

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Crystal structure of a phosphatase with a unique substrate binding domain fromThermotoga maritima

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Examination of the activity of carboxyl-terminal chimeric constructs of human and yeast ferrochelatases

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The penetrance of dominant erythropoietic protoporphyria is modulated by expression of wildtype FECH

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Metal binding to Saccharomyces cerevisiae ferrochelatase

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Porphyrin interactions with wild-type and mutant mouse ferrochelatase

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Functional Necessity and Physicochemical Characteristics of the [2Fe−2S] Cluster in Mammalian Ferrochelatase

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Probing the active-site residues in Saccharomyces cerevisiae ferrochelatase by directed mutagenesis. In vivo and in vitro analyses

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Substitution of murine ferrochelatase glutamate-287 with glutamine or alanine leads to porphyrin substrate-bound variants

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1 reference

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Alternative modes of substrate distortion in enzyme and antibody catalyzed ferrochelation reactions

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