This thesis describes the synthesis of new [Ni]- and [NiFe]-containing complexes as analogues of the active site of the [NiFe] hydrogenases and which have the potential as catalysis for the electro- or photochemical production of H2. The research described in the thesis focuses on two key aspects: (i) the modulation of the potential at which proton reduction may occur through the nature of the ligand about the metal centres and (ii) the incorporation of photosensitiser units into [Ni]- and [NiFe]-containing complexes. Chapter 1 provides an introduction to the [FeFe] and [NiFe] hydrogenases and provides the context for the research carried out in this thesis. Relevant coordination chemistry is surveyed with a focus on mononuclear and heter...
The photoproduction of dihydrogen (H2) by a low molecular weight analogue of the active site of [NiF...
NiFe hydrogenases are unique metalloenzymes that catalyze H+/H2 interconversion with remarkable effi...
Two model compounds of the active site of [NiFe]-hydrogenases with an unusual {S2Ni(μ-S)(μ-CO)Fe(CO)...
This thesis describes the synthesis of new [Ni]- and [NiFe]-containing complexes as analogues of the...
This thesis describes the syntheses and characterisations of heterobimetallic dithiolate complexes o...
This thesis reports the synthesis and the characterisation of functional analogues of the active sit...
Ni(L1)Fe(tBuNC)4](PF6)2 is a robust NiIIFeII complex that undergoes a reversible one-electron reduct...
The development of synthetic analogs of the active sites of [NiFe] hydrogenases remains challenging ...
The photoproduction of dihydrogen (H2) by a low molecular weight analogue of the active site of [NiF...
The development of synthetic analogs of the active sites of [NiFe] hydrogenases remains challenging ...
The hydrogenases are metalloenzymes that act to catalytically interconvert dihydrogen with protons a...
273 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2010.Unlike the [FeFe]-hydrogenase...
As humans continue to rely heavily on fossil fuels for our energy sources, many scientists are resea...
Hydrogenase enzymes reversibly catalyse the oxidation and production of hydrogen in a range close to...
The world's energy economy is driven by petroleum, but this resource is limited and its consumption ...
The photoproduction of dihydrogen (H2) by a low molecular weight analogue of the active site of [NiF...
NiFe hydrogenases are unique metalloenzymes that catalyze H+/H2 interconversion with remarkable effi...
Two model compounds of the active site of [NiFe]-hydrogenases with an unusual {S2Ni(μ-S)(μ-CO)Fe(CO)...
This thesis describes the synthesis of new [Ni]- and [NiFe]-containing complexes as analogues of the...
This thesis describes the syntheses and characterisations of heterobimetallic dithiolate complexes o...
This thesis reports the synthesis and the characterisation of functional analogues of the active sit...
Ni(L1)Fe(tBuNC)4](PF6)2 is a robust NiIIFeII complex that undergoes a reversible one-electron reduct...
The development of synthetic analogs of the active sites of [NiFe] hydrogenases remains challenging ...
The photoproduction of dihydrogen (H2) by a low molecular weight analogue of the active site of [NiF...
The development of synthetic analogs of the active sites of [NiFe] hydrogenases remains challenging ...
The hydrogenases are metalloenzymes that act to catalytically interconvert dihydrogen with protons a...
273 p.Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2010.Unlike the [FeFe]-hydrogenase...
As humans continue to rely heavily on fossil fuels for our energy sources, many scientists are resea...
Hydrogenase enzymes reversibly catalyse the oxidation and production of hydrogen in a range close to...
The world's energy economy is driven by petroleum, but this resource is limited and its consumption ...
The photoproduction of dihydrogen (H2) by a low molecular weight analogue of the active site of [NiF...
NiFe hydrogenases are unique metalloenzymes that catalyze H+/H2 interconversion with remarkable effi...
Two model compounds of the active site of [NiFe]-hydrogenases with an unusual {S2Ni(μ-S)(μ-CO)Fe(CO)...