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Homologous acetone carboxylases select Fe(II) or Mn(II) as the catalytic cofactor
by
Flusche, Tamara
, Mus, Florence
, Bothner, Brian
, Valaydon-Pillay, Adam
, Kincannon, William M.
, Raugei, Simone
, Kumar Nath, Arnab
, DuBois, Jennifer L.
, Stoian, Sebastian A.
, Peters, John W.
, Shisler, Krista A.
, Mattice, Jenna R.
, Larson, James
in
Acetoacetates
/ Acetone
/ Acetone - metabolism
/ Acids
/ Bacteria
/ Bicarbonates
/ Binding sites
/ Biological products
/ carboxylase
/ Catalysis
/ Chelation
/ CO2 fixation
/ Coordination Complexes
/ E coli
/ Enzymes
/ Ferrous Compounds - metabolism
/ Glycerol
/ Iron
/ Manganese
/ Manganese - metabolism
/ Metals
/ Metals - metabolism
/ Physiology and Metabolism
/ Post-translation
/ Preferences
/ Protein structure
/ Research Article
/ Transition metals
2024
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Homologous acetone carboxylases select Fe(II) or Mn(II) as the catalytic cofactor
by
Flusche, Tamara
, Mus, Florence
, Bothner, Brian
, Valaydon-Pillay, Adam
, Kincannon, William M.
, Raugei, Simone
, Kumar Nath, Arnab
, DuBois, Jennifer L.
, Stoian, Sebastian A.
, Peters, John W.
, Shisler, Krista A.
, Mattice, Jenna R.
, Larson, James
in
Acetoacetates
/ Acetone
/ Acetone - metabolism
/ Acids
/ Bacteria
/ Bicarbonates
/ Binding sites
/ Biological products
/ carboxylase
/ Catalysis
/ Chelation
/ CO2 fixation
/ Coordination Complexes
/ E coli
/ Enzymes
/ Ferrous Compounds - metabolism
/ Glycerol
/ Iron
/ Manganese
/ Manganese - metabolism
/ Metals
/ Metals - metabolism
/ Physiology and Metabolism
/ Post-translation
/ Preferences
/ Protein structure
/ Research Article
/ Transition metals
2024
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Homologous acetone carboxylases select Fe(II) or Mn(II) as the catalytic cofactor
by
Flusche, Tamara
, Mus, Florence
, Bothner, Brian
, Valaydon-Pillay, Adam
, Kincannon, William M.
, Raugei, Simone
, Kumar Nath, Arnab
, DuBois, Jennifer L.
, Stoian, Sebastian A.
, Peters, John W.
, Shisler, Krista A.
, Mattice, Jenna R.
, Larson, James
in
Acetoacetates
/ Acetone
/ Acetone - metabolism
/ Acids
/ Bacteria
/ Bicarbonates
/ Binding sites
/ Biological products
/ carboxylase
/ Catalysis
/ Chelation
/ CO2 fixation
/ Coordination Complexes
/ E coli
/ Enzymes
/ Ferrous Compounds - metabolism
/ Glycerol
/ Iron
/ Manganese
/ Manganese - metabolism
/ Metals
/ Metals - metabolism
/ Physiology and Metabolism
/ Post-translation
/ Preferences
/ Protein structure
/ Research Article
/ Transition metals
2024
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Homologous acetone carboxylases select Fe(II) or Mn(II) as the catalytic cofactor
Journal Article
Homologous acetone carboxylases select Fe(II) or Mn(II) as the catalytic cofactor
2024
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Overview
The Irving-Williams series refers to the predicted stabilities of transition metal complexes where the observed general stability for divalent first-row transition metal complexes increase across the row. Acetone carboxylases (ACs) use a coordinated divalent metal at their active site in the catalytic conversion of bicarbonate and acetone to form acetoacetate. Highly homologous ACs discriminate among different divalent metals at their active sites such that variations of the enzyme prefer Mn(II) over Fe(II), defying Irving-Williams-predicted behavior. Defining the determinants that promote metal discrimination within the first-row transition metals is of broad fundamental importance in understanding metal-mediated catalysis and metal catalyst design.
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