RT Journal Article
T1 Effect of Equatorial Ligand Substitution on the Reactivity with Proteins of Paddlewheel Diruthenium Complexes: Structural Studies
A1 Terán More, Aaron
A1 Ferraro, Giarita
A1 Sánchez Peláez, Ana Edilia
A1 Herrero Domínguez, Santiago
A1 Merlino, Antonello
AB The paddlewheel [Ru2Cl(O2CCH3)4] complex was previously reported to react with the model protein hen egg white lysozyme (HEWL), forming adducts with two diruthenium moieties bound to Asp101 and Asp119 side chains upon the release of one acetate. To study the effect of the equatorial ligands on the reactivity with proteins of diruthenium compounds, X-ray structures of the adducts formed when HEWL reacts with [Ru2Cl(D-p-FPhF)(O2CCH3)3] [D-p-FPhF = N,N′-bis(4-fluorophenyl)formamidinate] under different conditions were solved. [Ru2Cl(D-p-FPhF)(O2CCH3)3] is bonded through their equatorial positions to the Asp side chains. Protein binding occurs cis or trans to D-p-FPhF. Lys or Arg side chains or even main-chain carbonyl groups can coordinate to the diruthenium core at the axial site. Data help to understand the reactivity of paddlewheel diruthenium complexes with proteins, providing useful information for the design of new artificial diruthenium-containing metalloenzymes with potential applications in the fields of catalysis, biomedicine, and biotechnology.
PB American Chemical Society
SN 0020-1669
YR 2023
FD 2023
LK https://hdl.handle.net/20.500.14352/93056
UL https://hdl.handle.net/20.500.14352/93056
LA eng
NO Terán, Aarón, et al. «Effect of Equatorial Ligand Substitution on the Reactivity with Proteins of Paddlewheel Diruthenium Complexes: Structural Studies». Inorganic Chemistry, vol. 62, n.o 2, enero de 2023, pp. 670-74.  https://doi.org/10.1021/acs.inorgchem.2c04103.
DS Docta Complutense
RD 6 abr 2025