title: The hydrophilic phosphatriazaadamantane ligand in the development of H2 production electrocatalysts: iron hydrogenase model complexes.
abstract: As functional biomimics of the hydrogen-producing capability of the dinuclear active site in [Fe]H(2)ase, the Fe(I)Fe(I) organometallic complexes, (mu-pdt)[Fe(CO)(2)PTA](2), 1-PTA(2), (pdt = SCH(2)CH(2)CH(2)S; PTA = 1,3,5-triaza-7-phosphaadamantane), and (mu-pdt)[Fe(CO)(3)][Fe(CO)(2)PTA], 1-PTA, were synthesized and fully characterized. For comparison to the hydrophobic (mu-pdt)[Fe(CO)(2)(PMe(3))](2) and [(mu-H)(mu-pdt)[Fe(CO)(2)(PMe(3))](2)](+) analogues, electrochemical responses of 1-PTA(2) and 1-(PTA.H(+))(2) were recorded in acetonitrile and in acetonitrile/water mixtures in the absence and presence of acetic acid. The production of H(2) and the dependence of current on acid concentration indicated that the complexes were solution electrocatalysts that decreased over-voltage for H(+) reduction from HOAc in CH(3)CN by up to 600 mV. The most effective electrocatalyst is the asymmetric 1-PTA species, which promotes H(2) formation from HOAc (pK(a) in CH(3)CN = 22.6) at -1.4 V in CH(3)CN/H(2)O mixtures at the Fe(0)Fe(I) redox level. Functionalization of the PTA ligand via N-protonation or N-methylation, generating (mu-pdt)[Fe(CO)(2)(PTA-H(+))](2), 1-(PTA.H(+))(2), and (mu-pdt)[Fe(CO)(2)(PTA-CH(3)(+))](2), 1-(PTA-Me(+))(2), provided no obvious advantages for the electrocatalysis because in both cases the parent complex is reclaimed during one cycle under the electrochemical conditions and H(2) production catalysis develops from the neutral species. The order of proton/electron addition to the catalyst, i.e., the electrochemical mechanism, is dependent on the extent of P-donor ligand substitution and on the acid strength. Cyclic voltammetric curve-crossing phenomena was observed and analyzed in terms of the possible presence of an eta(2)-H(2)-Fe(II)Fe(I) species, derived from reduction of the Fe(I)Fe(I) parent complex to Fe(0)Fe(I) followed by uptake of two protons in an ECCE mechanism.
authors.affiliation: Department of Chemistry, Texas A&M University, College Station, Texas 77843, USA.
authors.forename: Rosario
authors.initials: R
authors.lastname: Mejia-Rodriguez
authors.forename: Daesung
authors.initials: D
authors.lastname: Chong
authors.forename: Joseph H
authors.initials: JH
authors.lastname: Reibenspies
authors.forename: Manuel P
authors.initials: MP
authors.lastname: Soriaga
authors.forename: Marcetta Y
authors.initials: MY
authors.lastname: Darensbourg
mesh_terms: D000218:Adamantane / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D040761:Biomimetic Materials / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D018360:Crystallography, X-Ray; D004563:Electrochemistry; D006859:Hydrogen / Q000378:metabolism*; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D058085:Iron Compounds / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D010084:Oxidation-Reduction
chemical_list: D058085:Iron Compounds; D007506:Iron-Sulfur Proteins; D006859:Hydrogen; C118830:iron hydrogenase; D006864:Hydrogenase; D000218:Adamantane