Treatment of Boc-protected (S)-serine (Ser) methyl ester with triphenylphosphine bromide Ph3PBr (intermittently generated from PPh3 and N-bromosuccinimide) yields Boc-3-bromoalanine (R)-Boc-BrAlaMe and, after deprotection, bromoalanine methyl ester (R)-BrAlaMe in the form of its hydrobromide. Boc-BrAlaMe and BrAlaMe have been structurally characterised. The reaction between BrAlaMe, salicylaldehyde (sal) and VO2+ results in the formation of Schiff base complexes of composition {[}VO(sal-BrAlaMe)solv](+) (solv = CH3OH: 3, THF: 5) and {[}VO(sal-BrAla)THF] 4. DFT calculations of the structures of 3, 4 and 5, based on the B3LYP functional and employing the triple zeta basis set 6-311++ g(d, p), provide distances Br center dot center dot center dot V = 4.0 + 0.1 angstrom, if some distortion of the dihedral angle. N-C-C-Br is allowed (affording a maximum energy of ca. 45 kJ mol(-1)), and thus model Br. V distances detected by X-ray methods in bromoperoxidases from the marine algae Ascophyllum nodosum and Corallina pilulifera. The DFT calculations have been validated by comparing calculated and found structures, including the new complex {[}(VO)-O-V(Amp-sal)OMe(MeOH)] (1, Amp is the aminophenol moiety) and the known complex {[}VO(L-Ser-van)H2O] (van = vanillin). Additional validation has been undertaken by checking experimental against calculated (BHandHLYP) EPR spectroscopic hyperfine coupling constants. Complexes containing bromine as a substituent at the phenyl moiety of a Schiff base ligand do not allow for an appropriate simulation of the Br. V distance in peroxidases. The closest agreement, d(Br center dot center dot center dot V) = 4.87 angstrom, is achieved with {[}VO(3Br-salSer)THF] (6), where 3Brsal-Ser is the dianionic Schiff base formed between 3-Br-5-NO2-salicylaldehyde and serine.