Specific derivatization of lysozyme in aqueous solution with Re(CO)3(H2O)3+

Abstract

The reaction of Re(CO)3(H2O)3+ with hen egg lysozyme in aqueous solution results in a single covalent adduct; single crystal X-ray diffraction shows that the rhenium tricarbonyl cation binds to His15 in two significantly populated rotamer conformations.

New insights into the chemistry of fac-[Ru(CO)3]2+ fragments in biologically relevant conditions: The CO releasing activity of [Ru(CO)3Cl2(1,3-thiazole)], and the X-ray crystal structure of its adduct with lysozyme

“…Several lysozyme structures accessible in the PDB exhibit transition metals bound to histidine 15 [9,[27][28][29]. As in those cases, the Ru-protein adduct shows a covalent bond between the metal and the Nε2 of the imidazole ring of the histidine side chain.…”

Characterization of a versatile organometallic pro-drug (CORM) for experimental CO based therapeutics

“…25 It is therefore surprising to realize that studies of the reactivity of metal carbonyl complexes with proteins are very scarce and contemplate only a handful of examples. 8, 44–46 …”

Reactions of [Re(CO)3]+ with Histidylhistidine and Modified Histidines

“…[20,21] When combined in histidine, they make for a tightly binding tridentate ligand whose compounds resist challenges at 37°C by biomolecular nucleophiles. [22] Comparison of imidazole Re-N δ bond lengths of 1-3 shows they are mostly similar, except that the Re-N δ bond length of the imidazole rings on the Nterminal histidine 3 is shorter by about 0.02 Å; presumably, this offsets the relatively weaker bonding of the amine group and the acyl oxygen atom.…”