Friday 11 October 2013, 12.15PM
Speaker(s): Dr Alison Parkin, Department of Chemistry, University of York
Hydrogenases are metalloenzymes produced by bacteria to catalyse H2-uptake and H2-production (H2D 2H++ 2e-). They are biotechnologically useful because they are the only H2-activating molecules which can compete with Pt in terms of catalytic efficiency and rate. Crucially, instead of containing a rare metal active site, hydrogenases contain Fe or NiFe reaction centres. The inhibitory reaction of hydrogenases with O2 is not only an important limiting factor in the potential human applications of these enzymes, it is also linked to the role which they play in bacterial metabolism. Escherichia coli produces up to four [NiFe]-hydrogenases and combined electrochemical, structural and molecular biology studies on hydrogenase-1 and hydrogenase-2 have helped elucidate the crucial role of electron-transfer in tuning the different O2-reactivity of these enzymes. Extending these studies to Salmonella hydrogenase-5 is now revealing further mechanistic details particularly related to the His-regulated function of a unique [4Fe3S(S-Cys)]-cluster.
Location: Dianna Bowles Lecture Theatre
Admission: All Welcome