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Literature summary for 1.16.3.2 extracted from

  • Bernacchioni, C.; Ciambellotti, S.; Theil, E.C.; Turano, P.
    Is His54 a gating residue for the ferritin ferroxidase site? (2015), Biochim. Biophys. Acta, 1854, 1118-1122 .
    View publication on PubMed
Search for more literature for 1.16.3.2

Protein Variants

Protein Variants Comment Organism
H54A site-directed mutagenesis, the mutant variant exhibits a 20% increase in the initial reaction rate of formation of ferric products with 2 or 4 Fe2+/subunit and higher than 200% with 20 Fe2+/subunit. The increased efficiency of the ferritin reaction induced by this mutation is proposed taking advantage of the comparative sequence analysis of other ferritins Lithobates catesbeianus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information stopped-flow kinetics Lithobates catesbeianus

Organism

Organism UniProt Comment Textmining
Lithobates catesbeianus
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information addition of 2 Fe2+ ions per subunit or 4 Fe2+ ions per subunit in frog wild-type or H54A mutant M ferritin. Recombinant ferritin protein cages are mineralized with ferrous sulfate, 20 Fe2+ ions per subunit. Fe2+ exit from caged ferritin minerals is initiated by reducing the ferritin mineral with added NADH and FMN and trapping the reduced and dissolved Fe2+ as the [Fe(2,2'-bipyridyl)3]2+ complex outside the protein cage. Fe2+ release from the protein cage is measured as the absorbance of [Fe(2,2'-bipyridyl)3]2+ at the maximum of A522 nm Lithobates catesbeianus ?
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 ?

Synonyms

Synonyms Comment Organism
M ferritin heavy subunit Lithobates catesbeianus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Lithobates catesbeianus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Lithobates catesbeianus

General Information

General Information Comment Organism
additional information role for His54 as a metal ion trap that maintains the correct levels of access of iron to the active site. His54 binding to iron(II) and other divalent cations, with its imidazole ring proposed as gate that influences iron movement to/from the active site. Lithobates catesbeianus