N. H. Yeung

Learn More
Metalloproteins catalyse some of the most complex and important processes in nature, such as photosynthesis and water oxidation. An ultimate test of our knowledge of how metalloproteins work is to design new metalloproteins. Doing so not only can reveal hidden structural features that may be missing from studies of native metalloproteins and their variants,(More)
The electrochemical properties of an engineered heme-copper center in myoglobin have been investigated by UV-visible spectroelectrochemistry. In the cyanide-bridged, spin-coupled heme-copper center in an engineered myoglobin, the presence of Zn(II) in the Cu(B) center raises the heme reduction potential from -85 to 49 mV vs NHE. However, in the(More)
The effects of metal ions on the reduction of nitric oxide (NO) with a designed heme copper center in myoglobin (F43H/L29H sperm whale Mb, CuBMb) were investigated under reducing anaerobic conditions using UV-vis and EPR spectroscopic techniques as well as GC/MS. In the presence of Cu(I), catalytic reduction of NO to N2O by CuBMb was observed with turnover(More)
Anisotropic conductive films (ACFs) received a great deal of attention in recent years for interconnection applications in electronic packaging. This paper reports the behaviour of ACF joints under various mechanical loading, i.e., die shear and cyclic fatigue in shear. The mechanical behaviour of ACF joints that have been exposed to environmental effects,(More)
Protein design provides a rigorous test of our knowledge about proteins and allows the creation of novel enzymes for biotechnological applications. Whereas progress has been made in designing proteins that mimic native proteins structurally, it is more difficult to design functional proteins. In comparison to recent successes in designing(More)
This paper reports that the stress-corrosion cracking induced by autoclave test condition reduces the mechanical strength of anisotropic conductive joints and also increases the contact resistance by allowing more moisture to reach the aluminium metallization. The use of anisotropic conductive joints with bumpless chips allows a reduction in the costs of(More)
A structural and functional model of bacterial nitric oxide reductase (NOR) has been designed by introducing two glutamates (Glu) and three histidines (His) in sperm whale myoglobin. X-ray structural data indicate that the three His and one Glu (V68E) residues bind iron, mimicking the putative Fe(B) site in NOR, while the second Glu (I107E) interacts with a(More)
Much progress has been made in designing metalloproteins with structures similar to native enzymes [1] and advances in computational biology have allowed for rational design of enzyme function as well. [2] Despite these achievements, most designed enzymes have simple active site structures and low activities, with limited turnover numbers. Designing(More)
The biosynthesis of iron sulfur (FeS) clusters, their trafficking from initial assembly on scaffold proteins via carrier proteins to final incorporation into FeS apoproteins, is a highly coordinated process enabled by multiprotein systems encoded in iscRSUAhscBAfdx and sufABCDSE operons in Escherichia coli. Although these systems are believed to encode all(More)