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Magnetic Properties
The magnetic properties of metal clusters are strongly influenced by their size and surface ligands. In general, the magnetic moments in small metal clusters are larger than in the case of a macroscopic bulk metal structure. For example, the average magnetic moment per atom in Ni clusters was found to be 0.7-0.8 μB, s compared with 0.6 μB for bulk Ni. This is explained by longer metal-metal bonds in cluster structures than in bulk structures, a consequence of a larger s character of metal-metal bonds in clusters. Magnetic moments approach bulk values as cluster size increases, though this is often difficult to predict computationally.

Magnetic quenching is an important phenomenon that is well documented for Ni clusters, and represents a significant effect of ligands on metal cluster magnetism. It has been shown that CO ligands cause the magnetic moments of surface Ni atoms to go to zero and the magnetic moment of inner Ni atoms to decrease to 0.5 μB. In this case, the 4s-derived Ni-Ni bonding molecular orbitals experience repulsion with the Ni-CO σ orbital, which causes its energy level to increase so that 3d-derived molecular orbitals are filled instead. Furthermore, Ni-CO π backbonding leaves Ni slightly positive, causing more transfer of electrons to 3d-derived orbitals, which are less disperse than those of 4s. Together, these effects result in a 3d10,diamagnetic character of the ligated Ni atoms, and their magnetic moment decreases to zero.

Density Functional Theory (DFT) calculations have shown that these ligand-induced electronic effects are limited to only surface Ni atoms, and inner cluster atoms are virtually unperturbed. Experimental findings have described two electronically distinct cluster atoms, inner atoms and surface atoms. These results indicate the significant effect that a cluster’s size has on its properties, magnetic and other.

Fe-Ni Clusters in Biology
Fe-Ni metal clusters are crucial for energy production in many bacteria. A primary source of energy in bacteria is the oxidation and reduction of H2 which is performed by hydrogenase enzymes. These enzymes which are able to create a charge gradient across the cell membrane which serves as an energy store. In aerobic environments, the oxidation and reduction of oxygen is the primary energy source. However, many bacteria are capable of living in environments where O2 supply is limited and use H2 as their primary energy source. The hydrogense enzymes which provide energy to the bacteria are centered around either a Fe-Fe or Fe-Ni active site. H2 metabolism is not used by humans or other complex life forms, but proteins in the mitochondria of mammalian life appear to have evolved from hydrogenase enzymes, indicating that hydrogenase is a crucial step in the evolutionary development of metabolism.



The active site of Fe-Ni containing hydrogenase enzymes often is composed of one or more bridging sulfur ligands, carbonyl, cyanide and terminal sulfur ligands. The non-bridging sulfur ligands are often cystine amino acid residues that attach the active site to the protein backbone. Metal-metal bonds between the Fe and Ni have not been observed. Several oxidation states of the Fe-Ni core have been observed in a variety of enzymes, though not all appear to be catalytically relevant.

The extreme oxygen and carbon monoxide sensitivity of these enzymes presents a challenge when studying the enzymes, but many crystallographic studies have been performed. Crystal structures for enzymes isolated from D. gigas, Desulfovibrio vulgaris, Desulfovibrio fructosovorans, Desulfovibrio desulfuricans, and Desulfomicrobium baculatum have been obtained, among others. A few bacteria, such as R. eutropha, have adapted to survive under ambient oxygen levels.

These enzymes have inspired study of structural and functional model complexes in hopes of making synthetic catalysis for hydrogen production (see Fe-Ni and Hydrogen Production, bellow, for more detail).

Fe-Ni and Hydrogen Production
In the search for a clean, renewable energy source to replace fossil fuels, hydrogen has gained much attention as a possible fuel for the future. One of the challenges that must be over come if this is to become a reality is an efficient way to produce and consume hydrogen. Currently, we have the technology to generate hydrogen from coal, natural gas, biomass and water. The majority of hydrogen currently produced comes from natural gas reformation, and hence does not help remove fossil fuel as an energy source. A variety of sustainable methods for hydrogen production are currently being researched, including solar, geothermal and catalytic hydrogen production.

Platinum is currently used to catalyze hydrogen production, but as Pt is expensive, found in limited supply, and easily poisoned by carbon monoxide during H2 production, it is not a practical for large-scale use. Catalysts inspired by the Fe-Ni active site of many hydrogen producing enzymes are particularly desirable due to the readily available and inexpensive metals.



The synthesis of Fe-Ni biomimetic catalytic complexes has proved difficult, primarily due to the extreme oxygen-sensitivity of such complexes. To date, only one example of a Fe-Ni model complex that is stable enough to withstand the range of electronic potential required for catalysis has been published.

When designing model complexes, it is crucial to preserve the key features of the active site of the Fe-Ni hydrogenases: the iron organometallic moiety with CO or CN- ligands, nickel coordinated to terminal sulfur ligands, and the thiolate bridge between the metals. By preserving these traits of the enzyme active site, it is hoped that the synthetic complexes will operate at the electrochemical potential necessary for catalysis, have a high turnover frequency and be robust.