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aci-reductone oxidase (CO-forming)

Known as: E2 metalloenzyme, acireductone dioxygenase 
 
National Institutes of Health

Papers overview

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2013
2013
Mononuclear Fe(II) complexes ([(6-Ph(2)TPA)Fe(PhC(O)C(R)C(O)Ph)]X (3-X: R = OH, X = ClO(4) or OTf; 4: R = H, X = ClO(4… Expand
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2011
2011
Heterotrimeric G protein complexes are conserved from plants to mammals, but the complexity of each system varies. Arabidopsis… Expand
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Highly Cited
2009
Highly Cited
2009
Crop plants require nitrogen for key macromolecules, such as DNA, proteins and metabolites, yet they are generally inefficient at… Expand
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2008
2008
The two acireductone dioxygenase (ARD) isozymes from the methionine salvage pathway of Klebsiella ATCC 8724 present an unusual… Expand
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2006
2006
Acireductone dioxygenase (ARD) catalyzes different reactions between O2 and 1,2-dihydroxy-3-oxo-5-(methylthio)pent-1-ene… Expand
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Highly Cited
2005
Highly Cited
2005
Methylthioadenosine (MTA) is formed as a by-product of ethylene biosynthesis from S-adenosyl-L-methionine (AdoMet). The… Expand
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2005
2005
The synthesis, characterization, and reactivity properties of a mononuclear Ni(II) cis-beta-keto-enolate complex, [(6-Ph2TPA)Ni… Expand
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2004
2004
The recent discovery of acireductone dioxygenase (ARD), a metalloenzyme containing a mononuclear octahedral Ni(II) center… Expand
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Highly Cited
2002
Highly Cited
2002
Here we report the structure of acireductone dioxygenase (ARD), the first determined for a new family of metalloenzymes. ARD… Expand
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2002
2002
Acireductone dioxygenases (ARDs) are enzymes involved in the methionine recycle pathway, which regulates aspects of the cell… Expand
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