GSTT SEMINAR: Prof Frank Sargent, University of Dundee - Title: 'Hydrogenases: enzymes of the past, enzymes of the future'
12:00pm - 1:00pm /
Monday 12th October 2015
Type: Seminar /
Category: Department
- Louise Crompton
- Admission: Free
- Book now
Add this event to my calendar
Click on "Create a calendar file" and your browser will download a .ics file for this event.
Microsoft Outlook: Download the file, double-click it to open it in Outlook, then click on "Save & Close" to save it to your calendar. If that doesn't work go into Outlook, click on the File tab, then on Open & Export, then Open Calendar. Select your .ics file then click on "Save & Close".
Google Calendar: download the file, then go into your calendar. On the left where it says "Other calendars" click on the arrow icon and then click on Import calendar. Click on Browse and select the .ics file, then click on Import.
Apple Calendar: The file may open automatically with an option to save it to your calendar. If not, download the file, then you can either drag it to Calendar or import the file by going to File >Import > Import and choosing the .ics file.
Frank Sargent is the Chair of Bacterial Physiology in the School of Life Sciences, University of Dundee, Scotland. He studied biochemistry at Edinburgh (1988-1992) before completing a PhD in Dundee (1992-1996). Following postdoctoral research at the John Innes Centre, Norwich (1996-1998) and the University of East Anglia (1998-2000), Frank started his own research group at the University of East Anglia thanks to the award of a Royal Society University Research Fellowship. Frank’s initial research focused on protein export and secretion in bacteria. In 2007, Frank returned to Dundee to form a new research Division of Molecular Microbiology. Here, his research took new directions, including studies of hydrogen metabolism by bacteria. As well as his research activities Frank is also a committed University teacher and was a winner of the Chancellor’s Award for Excellence in Teaching in 2014.
In this presentation, characterisation and engineering of [NiFe]-hydrogenases is discussed. The Escherichia coli genome encodes four [NiFe]-hydrogenases, termed Hyd-1 – Hyd-4. Two of these enzymes, Hyd-1 and Hyd-2, are predominantly involved in anaerobic respiration where they link hydrogen oxidation to quinone reduction. The Hyd-3 isoenzyme is part of the formate hydrogenlyase (FHL) complex that is produced under fermentative conditions and is the predominant source of the hydrogen gas produced by E. coli. FHL subunits share identity with Complex I subunits, which implicates FHL in a role as an energy-conserving ion pump. Moreover, evolutionary biologists hypothesise that progenitors of FHL may have been important enzymes on early Earth, where the ‘reverse’ activity could have linked H2 oxidation to CO2 reduction resulting in bioavailable formic acid. New genetic tools and assays establish that E. coli FHL is fully reversible both in vivo and in vitro, and the ability of E. coli to reduce CO2 to formate may be of biotechnological importance.
In this presentation, characterisation and engineering of [NiFe]-hydrogenases is discussed. The Escherichia coli genome encodes four [NiFe]-hydrogenases, termed Hyd-1 – Hyd-4. Two of these enzymes, Hyd-1 and Hyd-2, are predominantly involved in anaerobic respiration where they link hydrogen oxidation to quinone reduction. The Hyd-3 isoenzyme is part of the formate hydrogenlyase (FHL) complex that is produced under fermentative conditions and is the predominant source of the hydrogen gas produced by E. coli. FHL subunits share identity with Complex I subunits, which implicates FHL in a role as an energy-conserving ion pump. Moreover, evolutionary biologists hypothesise that progenitors of FHL may have been important enzymes on early Earth, where the ‘reverse’ activity could have linked H2 oxidation to CO2 reduction resulting in bioavailable formic acid. New genetic tools and assays establish that E. coli FHL is fully reversible both in vivo and in vitro, and the ability of E. coli to reduce CO2 to formate may be of biotechnological importance.