Understanding the Mechanism of Vanadium-Dependent Haloperoxidases and Related Biomimetic Catalysis

Schneider, Curtis J.; Zampella, Giuseppe; Degioa, Luca; Pecoraro, Vincent L.

doi:10.1021/bk-2007-0974.ch012

Cited by 11 publications

(8 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It has been shown that the catalytic mechanism is a bi-bi ping-pong two-substrate, where the first substrate (H 2 O 2 ) binds to the vanadate active site, forming a stable peroxovanadium complex and the first product (H 2 O) is released before the binding and oxidation, by the peroxo-intermediate, of the second substrate (X Cl − , Br − ) with the production of the oxidized halogenated intermediate (X + ) usually postulated as HOX [31,32]. These studies revealed a similar halide oxidation mechanism for the vanadium-containing enzymes.…”

Section: Discussionmentioning

confidence: 99%

Biocatalytic formation of synthetic melanin: The role of vanadium haloperoxidases, L-DOPA and iodide

Nicolai

Gonçalves

Natálio

et al. 2011

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Biocatalytic formation of synthetic melanin: The role of vanadium haloperoxidases, L-DOPA and iodide

Nicolai

Gonçalves

Natálio

et al. 2011

Journal of Inorganic Biochemistry

View full text Add to dashboard Cite

“…If the correct substrate is not present, the oxidized species can react with another equivalent of hydrogen peroxide to regenerate the halide and produce dioxygen in the singlet state . Whether hydrogen peroxide is the physiological halide oxidant has not been established, however, no other oxidants have yet been identified for V-HPOs and the V-HPO biochemistry has relied on using hydrogen peroxide in in vitro biochemical reactions . Unlike FDHs, crystal structures of V-HPOs have failed to reveal either the halide binding site, or the site at which substrates are bound by these enzymes.…”

Section: Vanadium-dependent Haloperoxidasesmentioning

confidence: 95%

“…189 Whether hydrogen peroxide is the physiological halide oxidant has not been established, however, no other oxidants have yet been identified for V-HPOs and the V-HPO biochemistry has relied on using hydrogen peroxide in in vitro biochemical reactions. 190 Unlike FDHs, crystal structures of V-HPOs have failed to reveal either the halide binding site, or the site at which substrates are bound by these enzymes. Moreover, the order of halide oxidation relative to substrate binding has not been revealed by kinetic studies.…”

Section: Vanadium-dependent Haloperoxidasesmentioning

confidence: 99%

Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse

et al. 2017

View full text Add to dashboard Cite

Naturally produced halogenated compounds are ubiquitous across all domains of life where they perform a multitude of biological functions and adopt a diversity of chemical structures. Accordingly, a diverse collection of enzyme catalysts to install and remove halogens from organic scaffolds has evolved in nature. Accounting for the different chemical properties of the four halogen atoms (fluorine, chlorine, bromine, and iodine) and the diversity and chemical reactivity of their organic substrates, enzymes performing biosynthetic and degradative halogenation chemistry utilize numerous mechanistic strategies involving oxidation, reduction, and substitution. Biosynthetic halogenation reactions range from simple aromatic substitutions to stereoselective C-H functionalizations on remote carbon centers and can initiate the formation of simple to complex ring structures. Dehalogenating enzymes, on the other hand, are best known for removing halogen atoms from man-made organohalogens, yet also function naturally, albeit rarely, in metabolic pathways. This review details the scope and mechanism of nature’s halogenation and dehalogenation enzymatic strategies, highlights gaps in our understanding, and posits where new advances in the field might arise in the near future.

show abstract

“…It is e.g. present in haloperoxidases as vanadium(V), 1–5 as vanadium(III) or vanadium(IV) complexes in tunicate blood cells. 6,7 and also as amavadine, a vanadium(IV) complex produced the mushroom genus Amanita .…”

Section: Introductionmentioning

confidence: 99%

“…20 The coordination chemistry and role of vanadium in biological systems have been reviewed in many publications and books. 1,5–10,21–23 Vanadium compounds have received increased attention as catalysts in a number of applications as recently reviewed. 24 …”

Section: Introductionmentioning

confidence: 99%

A Coordination Chemistry Study of Hydrated and Solvated Cationic Vanadium Ions in Oxidation States +III, +IV, and +V in Solution and Solid State

2012

View full text Add to dashboard Cite

The coordination chemistry of hydrated and solvated vanadium(III), oxovanadium(IV), and dioxovanadium(V) ions in the oxygen donor solvents water, dimethylsulfoxide (dmso) and N,N′-dimethylpropyleneurea (dmpu) has been studied in solution by EXAFS and large angle X-ray scattering (LAXS) and in solid state by single crystal X-ray diffraction and EXAFS. The hydrated vanadium(III) ion has a regular octahedral configuration with a mean V-O bond distance of 1.99 Å. In the hydrated and dimethylsulfoxide solvated oxovanadium(IV) ions vanadium binds strongly to an oxo group at ca. 1.6 Å. The solvent molecule trans to the oxo group is very weakly bound, at ca. 2.2 Å, while the remaining four solvent molecules, with a mean V-O bond distance of 2.0 Å, form a plane slightly below the vanadium atom; the mean O=V-Operp bond angle is ca. 98°. In the dmpu solvated oxovanadium(IV) ion, the space demanding properties of the dmpu molecule leaving no solvent molecule in the trans position to the oxo group which reduces the coordination number to 5. The O=V-O bond angle is consequently much larger, 106°, and the mean V=O and V-O bond distances decrease to 1.58 and 1.97 Å, respectively. The hydrated and dimethylsulfoxide solvated dioxovanadium(V) ions display a very distorted octahedral configuration with the oxo groups in cis position with mean V=O bond distances of 1.6 Å and a O=V=O bond angle of ca. 105°. The solvent molecules trans to the oxo groups are weakly bound, at ca. 2.2 Å, while the remaining two have bond distances of 2.02 Å. The experimental studies of the coordination chemistry of hydrated and solvated vanadium(III,IV,V) ions are complemented by summarizing previously reported crystal structures to yield a comprehensive description of the coordination chemistry of vanadium with oxygen donor ligands.

show abstract

Understanding the Mechanism of Vanadium-Dependent Haloperoxidases and Related Biomimetic Catalysis

Cited by 11 publications

References 0 publications

Biocatalytic formation of synthetic melanin: The role of vanadium haloperoxidases, L-DOPA and iodide

Biocatalytic formation of synthetic melanin: The role of vanadium haloperoxidases, L-DOPA and iodide

Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse

A Coordination Chemistry Study of Hydrated and Solvated Cationic Vanadium Ions in Oxidation States +III, +IV, and +V in Solution and Solid State

Contact Info

Product

Resources

About