Site-directed mutagenesis of dimethylsulfoxide reductase from Rhodobacter capsulatus: The critical roles of tyrosine-114 and tryptophan-116

The crystal structure of six functionally-distinct enzymes of the DMSO reductase family of molybdenum enzymes has revealed that the tertiary structure of the polypeptide that binds the bis(MGD)Mo cofactor is highly conserved. Differences in the catalytic properties of enzymes of this family are almost certainly dependent upon differences in the structure ofthe MO active site. In DMSO reductase from Rhodobacter species tryptophan- 116 (W 116) hydrogen-bonds to an 0x0 group coordinated to the MO ion. In addition a second amino acid side chain from tyrosine-114 (Y 114) is in close proximity to the 0x0 group. We have investigated the role of Y 114 and W 116 in DMSO reductase using site-directed mutagenesis,

Aboriginal and Torres Strait Islander Studies Unit Annual Report 2003

Welcome to the 2003 Aboriginal and Torres Strait Islander Studies Unit Annual Report. This report is a brief summary of Unit activities during the 2003 calendar year. The Unit provides personal and academic support for Aboriginal and Torres Strait Islander students and specifically aims to increase the recruitment, retention, academic performance and graduation rates of Indigenous students. The Unit also administers schemes to help Indigenous students gain access to, and receive support in, tertiary studies such as the Alternative Entry scheme and the federally funded Aboriginal Tutorial Assistance Scheme (ATAS). The Unit is also the focus for teaching and research in Aboriginal and Torres Strait Islander Studies at the University of Queensland.