1.11.1.18 Ba2+ activates 689414 1.11.1.18 Ca2+ activates 689414 1.11.1.18 Ca2+ contains one calcium atom per subunit 674916 1.11.1.18 Co2+ activates 689414 1.11.1.18 Cu2+ activates 689414 1.11.1.18 Fe2+ required 765465 1.11.1.18 Mg2+ activates 689414 1.11.1.18 Mn2+ activates 689414 1.11.1.18 additional information formation of mono- and dinuclear oxidovanadium(V) complexes of an amine-bis(phenolate) ligand with bromoperoxidase activities, synthetic routes and kinetics of the complexes, overview 764543 1.11.1.18 Ni2+ activates 689414 1.11.1.18 vanadate in the solid state structure, every protein monomer binds one vanadate to the tele imidazole nitrogen of residue His486. In solutions of sodium orthovanadate, isoform apobromoperoxidase II recovers bromoperoxidase activity by one order of magnitude faster than apobromoperoxidase I 726511 1.11.1.18 Vanadium - 765476 1.11.1.18 Vanadium contains 0.3 vanadium ions per subunit 671956 1.11.1.18 Vanadium contains 0.38 vanadium ions per subunit 671956 1.11.1.18 Vanadium dependent on 742111, 764730 1.11.1.18 Vanadium enzyme contains vanadium 671036, 672310, 673214 1.11.1.18 Vanadium presence of vanadium coordinated to oxygen/nitrogen either as vanadium(V) (in the native, native plus bromide, and native plus peroxide samples) or vanadium(IV) (in the reduced enzyme). There are structural changes at the metal site on reduction of the native enzyme, notably a lengthening of the average inner-shell distance and the presence of terminal oxygen together with histidine and oxygen-donating residues 671955 1.11.1.18 Vanadium required vanadium as a transition metal ion that readily converts among oxidations states has the potential to support catalytic processes through oxidation/reduction chemistry as well as hydrolytic chemistry. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview 765199 1.11.1.18 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 763808 1.11.1.18 Vanadium requires vanadium for enzyme activity. The enzyme activity increases ca. 250% with the action of V5+ on the isolated enzyme, since more than 2/3 of the protein molecules are in the apo form. This effect of V5+ addition is inhibited in phosphate buffer, probably because phosphate and vanadate compete for the active site 675244 1.11.1.18 Vanadium the enzyme contains vanadium 711546 1.11.1.18 Vanadium the holoenzyme contains trigonal-bipyramidal coordinated vanadium atoms at its two active centres 728120 1.11.1.18 Vanadium the substrate bromide does not bind to active site vanadium but to a light atom, possibly carbon, in its vicinity 675245 1.11.1.18 Vanadium the vanadium ion is ligated to the protein backbone via one histidine nitrogen donor atom, while the oxido moieties are strongly H-bonded to arginine, lysine, histidine and serine amino acids 764543 1.11.1.18 Vanadium vanadium-dependent enzyme 726562 1.11.1.18 VO43+ 1 mM, approximate doubling of activity 671929 1.11.1.18 VO43+ required 689414 1.11.1.18 Zn2+ activates 689414