We have synthesized two isostructural mononuclear cobalt(III) complexes [1]NO₃·3H₂O and [1]NO₃·CH₃CO₂H·H₂O {[1]₊ = [Co(1,10-phenanthroline)₂Cl₂]⁺} and characterized by single crystal X-ray structural analyses. Mass spectral studies of the complexes indicate both the compounds to produce identical cationic species viz., [Co(phen)₂Cl₂]⁺ in methanol solution. [1]⁺ has been evaluated as model system for the catechol oxidase enzyme by using 3,5-di-tert-butylcatechol (3,5-DTBC) as the substrate in methanol medium, which revealed that the cationic complex efficiently inhibits catalytic activity with k_cat value 9.65 × 10² h⁻¹. [1]⁺ cleaved pBR 322 DNA without addition of an activating agent. Further, the anti-cancer activity of [1]⁺ on human hepatocarcinoma cell line (HepG2) has been examined. The induction of apoptosis induced in the cell line was assessed base on the changes in cell morphology, which showed the efficacy of [1]⁺ to induce apoptosis in 53% of cells during 24 h treatment. Interestingly, the observed IC₅₀ values reveal that [1]⁺ brings about conformational change on DNA strongly and exhibits remarkable cytotoxicity.

A mononuclear cobalt(III) complex [Co(bpy)₂Cl₂]NO₃·2H₂O (1) (bpy = 2,2'-bipyridine) has been synthesized and crystallographically characterized. Self-assembly of the lattice water molecules from rectangular tetrameric water cluster interacts with nitrate anion along the c-axis forming a six membered hexagonal water-nitrate cluster. It presents a new mode of association of water molecules with nitrate molecules which is not predicted theoretically or found experimentally. The molecule effectively cleaves bacterial genomic DNA and shows important cytotoxicity against human hepatocarcinoma cell (HepG2).

An unprecedented solid of coper(II) complexes [Cu(dpa)₂NCS]₂[Cu(dpa)₂(NCS)₂](ClO₄)₂ (1) [dpa = 2,2'-dipyridylamine; SCN = thiocyanate], has been synthesized and crystallographically characterized with the aim to study the catecholase activity. The Cu(II) complex mimics the full catalytic cycle of the active site of catechol oxidase enzyme in acetonitrile medium with a turnover number of 4.788 × 10³ h⁻¹ along with the production of semiquinone radical and hydrogen peroxide. In situ generation of Cu(I) species in the catalytic pathway of catechol oxidation was established by electrochemical study and further confirmed by electron paramagnetic resonance (EPR) spectroscopy.

A mononuclear cobalt(II) complex, [Co(phen) ₂Cl ₂], (phen = 1,10-phenanthroline) has been synthesized and structurally characterized by different spectroscopic methods including single crystal X-ray structural study.X-ray crystal structural analysis revealed that the cobalt(II) complex crystallizes in amonoclinicsystem with C2/c space group and exists in cis-configuration in its crystalline state. Room temperature magnetic measurement accounts for 3e paramagnetism and indicates high spin cobalt(II) in the solid state. The cobalt(II) complex has been evaluated as a functional model for phosphatase enzyme by using 4-nitrophenylphosphate (PNPP) as a standard substrate in aqueous DMF medium. This mononuclear cobalt(II) complex exhibits good hydrolytic phosphoester cleavage efficiency with k_cat value of 3.78 × 10 ²h ⁻¹.

A coper(II) complex, [Cu(dpa)2(OAc)](ClO4) (1) [dpa =2, 2'-dipyridylamine; OAc = acetate], has been synthesized and crystallographically characterized. X-ray structure analysis revealed that this mononuclear Cu(II) complex crystallizes as a rare class of hexa coordination geometry named bicapped square pyramidalgeometry with P2₁/c space group. This copper complex displays excellent catalytic efficiency, k_cat /K_M (h⁻¹) = 6.17 × 10⁵ towards the oxidative coupling of 2-aminophenol (2-AP) to aminophenoxazin-3-one. Further, upon stoichiometric addition of copper(II) complex to 3,5-DTBC in presence of molecular oxygen in ethanol medium, the copper complex affords predominantly extradiol cleavage products along with a small amount of benzoquinone and a trace amount of intradiol cleavage products at a rate, k_obs = 1.09 × 10⁻³ min ⁻¹, which provide substantial evidence for the oxygen activation mechanism. This paper presents a novel addition of a copper(II) complex having the potential to mimic the active site of phenoxazinone synthase and catechol dioxygenase enzymes with significant catalytic efficiency.