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Literature summary for 1.16.3.1 extracted from

  • Kosman, D.J.
    Substrate entasis and electronic coupling elements in electron transfer from Fe in a multicopper ferroxidase (2008), Inorg. Chim. Acta, 361, 844-849.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.16.3.1

Protein Variants

Protein Variants Comment Organism
D283A X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 7-fold increase in Km value for Fe(II) Saccharomyces cerevisiae
D409A X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 4-fold increase in Km value for Fe(II) Saccharomyces cerevisiae
E185A X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 4-fold increase in Km value for Fe(II) Saccharomyces cerevisiae
E185A/D409A X-band cwEPR and near-uv and visible absorbance spectra quantitatively indistinguishable from wild type, 800-fold increase in Km value for Fe(II) Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.018
-
 hydroquinone mutant E185A Saccharomyces cerevisiae
0.019
-
 hydroquinone mutant D283A Saccharomyces cerevisiae
0.025
-
 hydroquinone wild-type Saccharomyces cerevisiae
0.03
-
 hydroquinone mutant D409A Saccharomyces cerevisiae
0.03
-
 hydroquinone mutant E185A/D409A Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Fe(II) wild-type, Km value 0.005 mM, mutant D283A, 0.019 mM, mutant E185A, 0.036 mM, mutant D409A, 0.019 mm, mutant E185A/D409A, 4 mM, respectively. The protein provides a binding site for Fe(II) that actually favors Fe(III), this coordination sphere places the bound Fe(II) in a state of entasis that can be relieved by loss of an electron. The EO of the bound Fe(II) is lowered relative to that of aqueous ferrous iron making electron transfer thermodynamically favorable. Carboxylates within this coordination sphere provide an electronic coupling pathway for the electron transfer via their H-bond network with type 1 Cu-histidine ligands thus making electron transfer kinetically efficient Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydroquinone + Fe2+ + O2
-
 Saccharomyces cerevisiae ?
-
 ?