Structural and mechanistic comparisons of the metal-binding members of the vicinal oxygen chelate (VOC) superfamily.

  title={Structural and mechanistic comparisons of the metal-binding members of the vicinal oxygen chelate (VOC) superfamily.},
  author={Panqing He and Graham R. Moran},
  journal={Journal of inorganic biochemistry},
  volume={105 10},
  • Panqing He, G. Moran
  • Published 4 July 2011
  • Chemistry, Biology
  • Journal of inorganic biochemistry
The Structure and Function Study of Three Metalloenzymes That Utilize Three Histidines as Metal Ligands
This study concluded that, H228Y not only plays a role of stabilizing and deprotonating the active site water but also is an essential residue on metal selectivity.
Imposing function down a (cupin)-barrel: secondary structure and metal stereochemistry in the αKG-dependent oxygenases.
The relationship between the chemical mechanism and the secondary coordination sphere of the αKG oxygenases, within the constraints of the stereochemistry of the Fe cofactor, is discussed.
Oxidative opening of the aromatic ring: Tracing the natural history of a large superfamily of dioxygenase domains and their relatives
Light is thrown on the functions of large swaths of the experimentally-uncharacterized PCAD–Memo families, extending known conserved contextual associations for the Memo clade beyond previously-described associations with the AMMECR1 domain and a radical S-adenosylmethionine family domain.
Molecular Basis for the Final Oxidative Rearrangement Steps in Chartreusin Biosynthesis.
ChaP is the first example of a dioxygenase that requires a flavin-activated oxygen as a substrate despite lacking flavin binding sites, and represents a new class in the vicinal oxygen chelate enzyme superfamily.
A new way of belonging: active-site investigation of L-DOPA dioxygenase, a VOC family enzyme from lincomycin biosynthesis.
It is demonstrated that the L-DOPA dioxygenase reaction depends upon an active site tyrosine and histidine and is remarkably resilient to mutation, even at the iron-ligating residues and Evaluation of the cleavage reaction as a function of pH supports the role of a histidine in acid-base catalysis.
Structural characterization of 2,6‐dichloro‐p‐hydroquinone 1,2‐dioxygenase (PcpA) from Sphingobium chlorophenolicum, a new type of aromatic ring‐cleavage enzyme
The site‐directed mutagenesis and kinetic analysis confirm the critical catalytic role played by the highly conserved His10, Thr13, His226 and Arg259, and propose a general reaction mechanism for p‐hydroquinone 1,2‐dioxygenases.
An iron (II) dependent oxygenase performs the last missing step of plant lysine catabolism
Structural and biochemical approaches are used to show that HglS acts via successive decarboxylation and intramolecular hydroxylation in a Fe(II)- and O 2 -dependent manner and that homologous enzymes catalyze the final step of lysine catabolism in plants.


Mechanistic diversity in a metalloenzyme superfamily.
An analysis of a metalloenzyme superfamily, the members of which catalyze a very diverse set of reactions with unrelated transition states but a more general common mechanistic imperative, is presented.
Crystallographic Comparison of Manganese- and Iron-Dependent Homoprotocatechuate 2,3-Dioxygenases
The X-ray crystal structures of homoprotocatechuate 2,3-dioxygenases isolated from Arthrobacter globiformis and Brevibacterium fuscum have been determined to high resolution, allowing the origins of metal ion selectivity and aspects of the molecular mechanism to be examined in detail.
Structural and functional comparison of 2-His-1-carboxylate and 3-His metallocentres in non-haem iron(II)-dependent enzymes.
The ability of the 2-His-1-carboxylate site to fit a site-directed substitution by an alternatively co-ordination or non-co-ordinating residue with retention of metal-binding capacity and catalytic function varies among different enzymes.
Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases.
The catalytic mechanism of the non-heme iron extradiol dioxygenases has been studied using hybrid density functional theory and the partly anionic character is found to determine the selectivity of the enzyme.
The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
General knowledge of dioxygen-activating mononuclear non-heme iron(II) enzymes containing a 2-His-1-carboxylate facial triad has significantly expanded in the last few years, due in large part to the
Crystal structure of human glyoxalase I—evidence for gene duplication and 3D domain swapping
Comparison of glyoxalase I with other known structures shows the enzyme to belong to a new structural family which includes the Fe2+‐dependent dihydroxybiphenyl dioxygenase and the bleomycin resistance protein, which appears to allow members to form with or without domain swapping.
Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent developments in enzymology and modeling studies.
This critical review aims to provide a concise background on the chemistry of the mononuclear non-heme iron enzymes characterized by the 2-His-1-carboxylate facial triad and to discuss the many recent developments in the field.
Structure-function correlations in oxygen activating non-heme iron enzymes.
A spectroscopic methodology has been developed which allows the elucidation of the geometric and electronic structures of these active sites and provides molecular level insight into the mechanisms of catalysis and its application to the determination of important active site structure-function correlations in mononuclear non-heme iron enzymes.
A density functional investigation of the extradiol cleavage mechanism in non-heme iron catechol dioxygenases
  • R. Deeth, T. Bugg
  • Chemistry
    JBIC Journal of Biological Inorganic Chemistry
  • 2003
The favoured proton-assisted pathway does not involve significant radical character and has features reminiscent of a Criegee rearrangement which involves the participation of the aromatic ring π-orbitals in the formation of the new carbon-oxygen bond.