H/D exchange reactions in dinuclear iron thiolates as activity assay models of Fe-H2ase.
Explore the source record for details and available documents.
Bacterial Proteins↗
Biomedical subjects
M Y Darensbourg
Publications and source records attributed to M Y Darensbourg.
Subtle bite-angle influences on N(2)S(2)Ni complexes.
A new N(2)S(2)Ni complex based on the 1,4-diazacycloheptane (dach) framework allows the study of the effects of ring size, in fused diamines, on the structural and chemical properties of nickel(II) dithiolate and dithioether complexes. Compared to its 1,5-diazacyclooctane (daco) derivatives, the dithiolate complex (bmedach)Ni and the S-templated, macrocyclic dithioether complex (propyl-bmedach)NiBr(2) show decreased cavity sizes with narrower angleN-Ni-N angles (by ca. 6 degrees ) and wider angleS-Ni-S angles (also by ca. 6 degrees ). The electrochemical properties of the dithiolate complexes based on dach and daco are nearly identical, while the (propyl-bmedach)NiBr(2) complex shows a 140 mV destabilization of the Ni(I) oxidation state relative to its daco analogue. Molecular structures for the (bmedach)Ni and (propyl-bmedach)NiBr(2) complexes and their respective electrochemical and spectroscopic properties are reported.
Journal Article↗
Coordination sphere flexibility of active-site models for Fe-only hydrogenase: studies in intra- and intermolecular diatomic ligand exchange.
A series of dinuclear complexes, (mu-SRS)Fe(2)(CO)(6) (R = -CH(2)CH(2)-, -CH(2)CH(2)CH(2)-, -CH(2)-C(6)H(4)-CH(2)-; edt, pdt, and o-xyldt, respectively) has been examined for specific characteristics that might relate to structural similarity with the active site of Fe-only hydrogenases. Variable-temperature proton NMR studies display the fluxionality of the iron-dithiocyclohexane unit in (mu-pdt)Fe(2)(CO)(6) while in the (mu-o-xyldt)Fe(2)(CO)(6) compound, the bridge is fixed. Temperature-dependent (13)C NMR spectral studies establish intramolecular CO site exchange localized on discrete Fe(CO)(3) units in all complexes, which is influenced by steric effects of the mu-SRS unit. Kinetic studies of intermolecular CO/CN(-) ligand-exchange reactions establish associative or I(a) mechanisms in sequential steps to form the dicyano dianion, (mu-SRS)[Fe(CO)(2)(CN)](2)(=) with 100% selectivity. Theoretical calculations (DFT) of transition states in the intramolecular site-exchange processes lead to a rationale for the interesting cooperativity in the CN(-)/CO intermolecular ligand-exchange process. The hinge motion of the three light atom S-to-S bridge is related to a possible heterolytic H(2) activation/production process in the enzyme.
Binding Sites↗
Heterobimetallics of nickel-iron dinitrosyl: electronic control by chelate and diatomic ligands.
Reaction of [PPN][Fe(NO)2(SePh)2] (1) with dimeric [Ni(mu-SCH2CH2SCH2CH2S)]2 in the presence of additional NO2- produced the neutral heterobimetallic [(ON)Ni[(mu-SCH2CH2)2S]Fe(NO)2] complex (2). The X-ray crystal structures of 1 and 2 show distorted tetrahedral iron dinitrosyl groups, assigned according to the Feltham-Enemark notation as [Fe(NO)2]9 The Fe-NO bonds are off linearity by an average of approximately equals 10 degrees for compounds 1 and 2, while a more linear Ni-NO coordination with a Ni-NO distance of 1.644(2) A was found in 2. The v(NO) value of complex 2 is consistent with an assignment for [Ni(NO)]9 of Ni0(NO)+ as is known for analogous phosphine derivatives, P3Ni0(NO)+. EPR signals of g values = 2.02-2.03 confirmed the existence of the odd electron in the chalcogenated [Fe(NO)2]9 compounds. Two [Fe(NO)2]10 complexes coordinated by the nickel(II) dithiolate, (bismercaptoethanediazacyclooctane)nickel(II), (Ni-1), (Ni-1)Fe(CO)(NO)2 and (Ni-1)Fe(NO)2, were prepared for comparison to the Ni0(NO)+ derivative and other monomeric and homodimetallic derivatives of the Fe(NO)2 fragment. While the oxidation level of Fe(NO)2 is the primary determinant of v(NO) values, they are also highly sensitive to ancillary ligands and, thereby, the distal metal influence through the bridging thiolate donor.
Binding Sites↗