Inorganic

Novel Heme Proteins and Model Systems (#305)

Heme proteins contain iron porphyrin as a cofactor and are abundant in living organisms. They provide the function in countless enzymes, with functional examples including gas-carriers and sensors and as transcriptional regulators. For decades, investigations of heme proteins have paved the way to our current knowledge of how metal ions in general function in Nature. These detailed studies continue today with the aid of new technologies that shed new light on the structure and function of these proteins. Recent discoveries report heme proteins playing new functional roles in biological systems. The development of structural and functional model heme systems has also been important in achieving our present knowledge of how naturally occurring heme iron systems work. This symposium will highlight recent exciting developments in the field. Topics will include lectures reporting studies on: (1) heme transport proteins, (2) heme-dependent gas sensors, (3) heme-containing transcription regulators, (4) mechanistic studies on heme enzymes such as cytochrome P450, cytochrome c oxidase, and nitric oxide synthase, and (5) artificially modified heme proteins and synthetically generated heme complexes created to produce new bio-inspired metalloporphyrin catalysts and/or materials.
Last update: Dec 28, 2015