Dataset Information

Ferrous Carbonyl Dithiolates as Precursors to FeFe, FeCo, and FeMn Carbonyl Dithiolates.

ABSTRACT: Reported are complexes of the formula Fe(dithiolate)(CO)2(diphos) and their use to prepare homo- and heterobimetallic dithiolato derivatives. The starting iron dithiolates were prepared by a one-pot reaction of FeCl2 and CO with chelating diphosphines and dithiolates, where dithiolate = S2(CH2)2(2-) (edt(2-)), S2(CH2)3(2-) (pdt(2-)), S2(CH2)2(C(CH3)2)(2-) (Me2pdt(2-)) and diphos = cis-C2H2(PPh2)2 (dppv), C2H4(PPh2)2 (dppe), C6H4(PPh2)2 (dppbz), C2H4[P(C6H11)2]2 (dcpe). The incorporation of (57)Fe into such building block complexes commenced with the conversion of (57)Fe into (57)Fe2I4( (i) PrOH)4, which then was treated with K2pdt, CO, and dppe to give (57)Fe(pdt)(CO)2(dppe). NMR and IR analyses show that these complexes exist as mixtures of all-cis and trans-CO isomers, edt(2-) favoring the former and pdt(2-) the latter. Treatment of Fe(dithiolate)(CO)2(diphos) with the Fe(0) reagent (benzylideneacetone)Fe(CO)3 gave Fe2(dithiolate)(CO)4(diphos), thereby defining a route from simple ferrous salts to models for hydrogenase active sites. Extending the building block route to heterobimetallic complexes, treatment of Fe(pdt)(CO)2(dppe) with [(acenaphthene)Mn(CO)3](+) gave [(CO)3Mn(pdt)Fe(CO)2(dppe)](+) ([3d(CO)](+)). Reduction of [3d(CO)](+) with BH4(-) gave the Cs -symmetric ?-hydride (CO)3Mn(pdt)(H)Fe(CO)(dppe) (H3d). Complex H3d is reversibly protonated by strong acids, the proposed site of protonation being sulfur. Treatment of Fe(dithiolate)(CO)2(diphos) with CpCoI2(CO) followed by reduction by Cp2Co affords CpCo(dithiolate)Fe(CO)(diphos) (4), which can also be prepared from Fe(dithiolate)(CO)2(diphos) and CpCo(CO)2. Like the electronically related (CO)3Fe(pdt)Fe(CO)(diphos), these complexes undergo protonation to afford the ?-hydrido complexes [CpCo(dithiolate)HFe(CO)(diphos)](+). Low-temperature NMR studies indicate that Co is the kinetic site of protonation.

SUBMITTER: Carroll ME

PROVIDER: S-EPMC3999794 | biostudies-other | 2014 Feb

REPOSITORIES: biostudies-other

ACCESS DATA

Publications

Ferrous Carbonyl Dithiolates as Precursors to FeFe, FeCo, and FeMn Carbonyl Dithiolates.

Carroll Maria E ME Chen Jinzhu J Gray Danielle E DE Lansing James C JC Rauchfuss Thomas B TB Schilter David D Volkers Phillip I PI Wilson Scott R SR

Organometallics 20140203 4

Reported are complexes of the formula Fe(dithiolate)(CO)2(diphos) and their use to prepare homo- and heterobimetallic dithiolato derivatives. The starting iron dithiolates were prepared by a one-pot reaction of FeCl2 and CO with chelating diphosphines and dithiolates, where dithiolate = S2(CH2)22- (edt2-), S2(CH2)32- (pdt2-), S2(CH2)2</sub ...[more]

PMID: 24803716

Similar Datasets

Project description:A non-bifurcating NADH-dependent, dimeric [FeFe]-hydrogenase (HydAB) from Syntrophus aciditrophicus was heterologously produced in Escherichia coli, purified and characterized. Purified recombinant HydAB catalyzed NAD+ reduction coupled to hydrogen oxidation and produced hydrogen from NADH without the involvement of ferredoxin. Hydrogen partial pressures (2.2-40.2 Pa) produced by the purified recombinant HydAB at NADH to NAD+ ratios of 1-5 were similar to the hydrogen partial pressures generated by pure and cocultures of S. aciditrophicus (5.9-36.6 Pa). Thus, the hydrogen partial pressures observed in metabolizing cultures and cocultures of S. aciditrophicus can be generated by HydAB if S. aciditrophicus maintains NADH to NAD+ ratios greater than one. The flavin-containing beta subunits from S. aciditrophicus HydAB and the non-bifurcating NADH-dependent S. wolfei Hyd1ABC share a number of conserved residues with the flavin-containing beta subunits from non-bifurcating NADH-dependent enzymes such as NADH:quinone oxidoreductases and formate dehydrogenases. A number of differences were observed between sequences of these non-bifurcating NADH-dependent enzymes and [FeFe]-hydrogenases and formate dehydrogenases known to catalyze electron bifurcation including differences in the number of [Fe-S] centers and in conserved residues near predicted cofactor binding sites. These differences can be used to distinguish members of these two groups of enzymes and may be relevant to the differences in ferredoxin-dependence and ability to mediate electron-bifurcation. These results show that two phylogenetically distinct syntrophic fatty acid-oxidizing bacteria, Syntrophomonas wolfei a member of the phylum Firmicutes, and S. aciditrophicus, a member of the class Deltaproteobacteria, possess functionally similar [FeFe]-hydrogenases that produce hydrogen from NADH during syntrophic fatty acid oxidation without the involvement of reduced ferredoxin. The reliance on a non-bifurcating NADH-dependent [FeFe]-hydrogenases may explain the obligate requirement that many syntrophic metabolizers have for a hydrogen-using partner microorganism when grown on fatty, aromatic and alicyclic acids.

Dataset Information

Ferrous Carbonyl Dithiolates as Precursors to FeFe, FeCo, and FeMn Carbonyl Dithiolates.

Publications

Ferrous Carbonyl Dithiolates as Precursors to FeFe, FeCo, and FeMn Carbonyl Dithiolates.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure