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Literature summary for 1.11.1.B2 extracted from

  • Anderson, G.A.; Behera, R.N.; Gomatam, R.
    Calculation of higher protonation states and of a new resting state for vanadium chloroperoxidase using QM/MM, with an atom-in-molecules analysis (2020), J. Mol. Graph. Model., 99, 107624 .
    View publication on PubMed
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Metals/Ions

Metals/Ions Comment Organism Structure
Vanadium required, electronic structure of the vanadate protonation states, overview Curvularia inaequalis

Organism

Organism UniProt Comment Textmining
Curvularia inaequalis P49053 Helminthosporium inaequale
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Synonyms

Synonyms Comment Organism
More cf. EC 1.11.1.10 Curvularia inaequalis
vanadium chloroperoxidase
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 Curvularia inaequalis
vCPO
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 Curvularia inaequalis

Cofactor

Cofactor Comment Organism Structure
vanadate cofactor complex hydrogen bonding around the vanadate cofactor, Atoms-in-molecules (AIM) analysis Curvularia inaequalis

General Information

General Information Comment Organism
additional information calculation of higher protonation states and of a distict resting state for vanadium chloroperoxidase using quantum mechanics/molecular mechanics (QM/MM), with an atom-in-molecules analysis, overview. Di- and triprotonated states are identified as being candidates for the resting state based on a comparison of relative energies. The quadprotonated states as well as some of the triprotonated states are ruled out as the resting state. Structure of the active site of vanadium chloroperoxidase (VCPO) with bound vanadate cofactor in an unprotonated state Curvularia inaequalis