Literature summary for 1.11.1.18 extracted from

Radlow, M.; Czjzek, M.; Jeudy, A.; Dabin, J.; Delage, L.; Leblanc, C.; Hartung, J.
X-ray diffraction and density functional theory provide insight into vanadate binding to homohexameric bromoperoxidase II and the mechanism of bromide oxidation (2018), ACS Chem. Biol., 13, 1243-1259 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified native enzyme, hanging drop vapor diffusion method, mixing of 0.001-0.002 ml of 8 mg/ml protein solution with 0.0005-0.001 ml of reservoir solution containing 0.1 M sodium chloride, 0.01 M Tris-HCl, pH 5.5, and 25% PEG 3350 leading to monoclinic crystals, or 0.15 M potassium rhodanide, 0.01 M Tris, pH 7.5, and 19% PEG 3350 leading to hexagonal crystals, both at a temperature of 18°C, X-ray diffraction structure determination and analysis at 2.26 A resolution, molecular replacement and modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template	Ascophyllum nodosum

Crystallization (Comment)

Organism

purified native enzyme, hanging drop vapor diffusion method, mixing of 0.001-0.002 ml of 8 mg/ml protein solution with 0.0005-0.001 ml of reservoir solution containing 0.1 M sodium chloride, 0.01 M Tris-HCl, pH 5.5, and 25% PEG 3350 leading to monoclinic crystals, or 0.15 M potassium rhodanide, 0.01 M Tris, pH 7.5, and 19% PEG 3350 leading to hexagonal crystals, both at a temperature of 18°C, X-ray diffraction structure determination and analysis at 2.26 A resolution, molecular replacement and modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template

Ascophyllum nodosum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Vanadium	required, every monomer binds one equivalent of orthovanadate in a cavity formed from side chains of three histidines, two arginines, one lysine, serine, and tryptophan	Ascophyllum nodosum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
RH + Br- + H2O2 + H+	Ascophyllum nodosum	-	RBr + 2 H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Ascophyllum nodosum	K7ZUA3	-	-

Purification (Commentary)

Purification (Comment)	Organism
native enzyme VBrPO(AnII) from algal powder by liquid-liquid-partitioning, dialysis, and ultracentrifugation	Ascophyllum nodosum

Reaction

Reaction	Comment	Organism	Reaction ID
RH + HBr + H2O2 = RBr + 2 H2O	proposed states at the bromoperoxidase active site involved in primary product formation and secondary reaction consuming hypobromous acid in the absence of an accepting organic substrate, overview. At the bromoperoxidase II binding site, dihydrogen orthovanadate most likely encounters reactivity in between diffusion-controlled solution chemistry and aligned reactant pairs. According to steady kinetic data, hydrogen peroxide binding to VBrPO(AnII) is one of the rate-determining steps. The energy required for transforming the bromoperoxidase resting state into the peroxo state must be provided by the succeeding step, which is the transfer of a peroxide oxygen atom to bromide. The least negatively charged oxygen in peroxide side-on-4, OP, is the site preferentially approached by bromide in the electronic structure model. Reaction mechanism analysis	Ascophyllum nodosum	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	protein binding through the enzyme occurs primarily through hydrogen bridges and superimposed by Coulomb attraction according to thermochemical model on density functional level of theory. The strongest attractor is the arginine side chain mimic N-methylguanidinium, enhancing in positive cooperative manner hydrogen bridges toward weaker acceptors, such as residues from lysine and serine. Hydrogen peroxide activation occurs in the thermochemical model by side-on binding in orthovanadium peroxoic acid, oxidizing bromide with virtually no activation energy to hydrogen bonded hypobromous acid	Ascophyllum nodosum	?	-	-
RH + Br- + H2O2 + H+	-	Ascophyllum nodosum	RBr + 2 H2O	-	?

Subunits

Subunits	Comment	Organism
homohexamer	bromoperoxidase II comprises six identical subunits. Converging chains of N-terminal peptides are interwoven at dimer-dimer interfaces in a catenane-type manner. Guanidinium stacks between arginine side chains tighten interfaces by hydrogen bond-clamping between prolyl carboxamide and guanidinium groups, being supplemented by attractive forces from arrays of hydrogen-bonded water molecules, for overcoming like/like repulsion. 40% of the bromoperoxidase II solid state secondary structure derive from helices, 10% from beta-strands, 4% from turns, and 46% from coils. Primary and secondary enzyme structure analysis, comparison of the enzyme structure with other enzyme structures, modeled surface polarization of a VBrPO(AnII)-monomer, detailed overview. Every chain, labeled alphabetically from A to F, contains one molecule of orthovanadate. Disulfide bridges connect thiol groups from cysteine(Cys)41 and Cys77 of one chain to Cys77 and Cys41 to the proximal, linking chain A to chain F, B to C, and D to E. Intramolecular disulfide bridges are formed from Cys117 to Cys126, from Cys474 to Cys502, and from Cys603 to Cys613	Ascophyllum nodosum

Synonyms

Synonyms	Comment	Organism
bromoperoxidase II	-	Ascophyllum nodosum
vanadium-dependent bromoperoxidase 2	-	Ascophyllum nodosum
VBPO2	-	Ascophyllum nodosum
VBrPO(AnII)	-	Ascophyllum nodosum

Cofactor

Cofactor	Comment	Organism	Structure
additional information	development of a comprehensive theory for cofactor bonding and bromide oxidation at the active site using an assessed electronic structure method. Three dimers interwoven in contact regions and tightened by hydrogen-bond-clamped guanidinium stacks along with regularly aligned water molecules form the basic structure of the enzyme. Intra- and intermolecular disulfide bridges further stabilize the enzyme	Ascophyllum nodosum
vanadate cofactor	required, binding structure and thermodynamics analysis, detailed overview. Every monomer binds one equivalent of orthovanadate in a cavity formed from side chains of three histidines, two arginines, one lysine, serine, and tryptophan. Hydrogen peroxide interferes with orthovanadate equilibria, providing in pH-neutral aqueous solution mono-, di-, tri-, and tetraperoxidoorthovanadates, depending on concentration and vanadate-peroxide ratio. Bromoperoxidase proteins control specificity for oxygen atom transfer to bromide to give hypobromous acid and direct the cofactor by the end of the sequence into the resting state for resuming substrate turnover in a succeeding catalytic cycle. Calculated energies for isodesmic substitution of water from hydrated orthovanadates via vanadium bonding of nitrogen compounds	Ascophyllum nodosum

General Information

General Information	Comment	Organism
evolution	the enzyme belongs into a class of metalloenzymes utilizing orthovanadate as a cofactor for activating hydrogen peroxide	Ascophyllum nodosum
additional information	analysis of cofactor bonding and bromide oxidation at the active site, overview. Three-dimensional structure modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template	Ascophyllum nodosum
physiological function	the peroxide is the terminal oxidant for converting bromide into electrophilic bromine compounds	Ascophyllum nodosum