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Dr Elizabeth Dridge

Dr Elizabeth Dridge

Project Manager (Space)

 2347

 Geoffrey Pope 313

 

Geoffrey Pope Building, University of Exeter , Stocker Road, Exeter, EX4 4QD, UK

Overview

I am currently employed at Exeter University as an Associate Lecturer and Associate Research Fellow. As a lecturer I am module leader for BIO1325 ‘Introduction to Biotechnology’ and lecture on various additional modules, covering molecular biology, biochemistry and metabolism. My research interests lie in microbial biochemistry and metabolism.

My current research post, funded by Shell, is investigating the colonial microalga Botryococcus braunii as a potential source for biofuel production.

My previous BBSRC funded post doctoral position and PhD focused on bacterial respiration pathways, looking mainly at the putative nitrate/selenate reductase in Archaeoglobus fulgidus and the selenate reductase in Thauera selenatis. Further work on T. selenatis also included investigations in how the organism was able to reduce soluble selenate to the insoluble precipitate selenium, and its role in biomineralisation. I am also the post-doctoral representative for Biosciences at Streatham.

Research Specialisms

  • Microbial biochemistry
  • microbiology
  • bioenergetics
  • algal biofuel
  • photo-bioreactor growth of algal cultures.

Qualifications

PhD (2007) Newcastle University Molecular analysis of the Type II molybdo-enzymes from Thauera selenatis and Archaeoglobus fulgidus.
BSc Hons (2003) Newcastle University Biomedical Sciences

Career

2007 – 2009 BBSRC funded Associate Research Fellow – University of Exeter
2009 – present Shell funded Associate Research Fellow – University of Exeter
2011 – present Associate Lecturer – University of Exeter

Research

Publications

Key publications | Publications by category | Publications by year

Publications by category


Journal articles

Debieux CM, Dridge EJ, Mueller CM, Splatt P, Paszkiewicz K, Knight I, Florance H, Love J, Titball RW, Lewis RJ, et al (2011). A bacterial process for selenium nanosphere assembly. Proc Natl Acad Sci U S A, 108(33), 13480-13485. Abstract.  Author URL.
Lowe EC, Bydder S, Hartshorne RS, Tape HLU, Dridge EJ, Debieux CM, Paszkiewicz K, Singleton I, Lewis RJ, Santini JM, et al (2010). Quinol-cytochrome c oxidoreductase and cytochrome c4 mediate electron transfer during selenate respiration in Thauera selenatis. J Biol Chem, 285(24), 18433-18442. Abstract.  Author URL.
Lowe EC, Bydder S, Hartshorne RS, Tape HLU, Dridge EJ, Debieux CM, Paszkiewicz K, Singleton I, Lewis RJ, Santini JM, et al (2010). Quinol-cytochrome c oxidoreductase and cytochrome c<inf>4</inf> mediate electron transfer during selenate respiration in Thauera selenatis. Journal of Biological Chemistry, 285(24), 18433-18442. Abstract.
Dridge EJ, Butler CS (2010). Thermostable properties of the periplasmic selenate reductase from Thauera selenatis. Biochimie, 92(10), 1268-1273. Abstract.  Author URL.
Dridge EJ, Watts CA, Jepson BJN, Line K, Santini JM, Richardson DJ, Butler CS (2007). Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy. Biochem J, 408(1), 19-28. Abstract.  Author URL.
Martinez-Espinosa RM, Dridge EJ, Bonete MJ, Butt JN, Butler CS, Sargent F, Richardson DJ (2007). Look on the positive side! the orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases. FEMS Microbiol Lett, 276(2), 129-139. Abstract.  Author URL.
Dridge EJ, Richardson DJ, Lewis RJ, Butler CS (2006). Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: Application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus. Biochemical Society Transactions, 34(1), 118-121. Abstract.
Ridley, H. Dridge, E.J. Leaver, J.T. (2005). Microbial reduction of selenate and nitrate: Common themes and variations. Biochemical Society Transactions, 33, 173-175.

Conferences

Dridge EJ, Richardson DJ, Lewis RJ, Butler CS (2006). Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus.  Abstract.  Author URL.
Watts CA, Ridley H, Dridge EJ, Leaver JT, Reilly AJ, Richardson DJ, Butler CS (2005). Microbial reduction of selenate and nitrate: common themes and variations.  Abstract.  Author URL.

Publications by year


2011

Debieux CM, Dridge EJ, Mueller CM, Splatt P, Paszkiewicz K, Knight I, Florance H, Love J, Titball RW, Lewis RJ, et al (2011). A bacterial process for selenium nanosphere assembly. Proc Natl Acad Sci U S A, 108(33), 13480-13485. Abstract.  Author URL.

2010

Lowe EC, Bydder S, Hartshorne RS, Tape HLU, Dridge EJ, Debieux CM, Paszkiewicz K, Singleton I, Lewis RJ, Santini JM, et al (2010). Quinol-cytochrome c oxidoreductase and cytochrome c4 mediate electron transfer during selenate respiration in Thauera selenatis. J Biol Chem, 285(24), 18433-18442. Abstract.  Author URL.
Lowe EC, Bydder S, Hartshorne RS, Tape HLU, Dridge EJ, Debieux CM, Paszkiewicz K, Singleton I, Lewis RJ, Santini JM, et al (2010). Quinol-cytochrome c oxidoreductase and cytochrome c<inf>4</inf> mediate electron transfer during selenate respiration in Thauera selenatis. Journal of Biological Chemistry, 285(24), 18433-18442. Abstract.
Dridge EJ, Butler CS (2010). Thermostable properties of the periplasmic selenate reductase from Thauera selenatis. Biochimie, 92(10), 1268-1273. Abstract.  Author URL.

2007

Dridge EJ, Watts CA, Jepson BJN, Line K, Santini JM, Richardson DJ, Butler CS (2007). Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy. Biochem J, 408(1), 19-28. Abstract.  Author URL.
Martinez-Espinosa RM, Dridge EJ, Bonete MJ, Butt JN, Butler CS, Sargent F, Richardson DJ (2007). Look on the positive side! the orientation, identification and bioenergetics of 'Archaeal' membrane-bound nitrate reductases. FEMS Microbiol Lett, 276(2), 129-139. Abstract.  Author URL.

2006

Dridge EJ, Richardson DJ, Lewis RJ, Butler CS (2006). Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: Application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus. Biochemical Society Transactions, 34(1), 118-121. Abstract.
Dridge EJ, Richardson DJ, Lewis RJ, Butler CS (2006). Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus.  Abstract.  Author URL.

2005

Ridley, H. Dridge, E.J. Leaver, J.T. (2005). Microbial reduction of selenate and nitrate: Common themes and variations. Biochemical Society Transactions, 33, 173-175.
Watts CA, Ridley H, Dridge EJ, Leaver JT, Reilly AJ, Richardson DJ, Butler CS (2005). Microbial reduction of selenate and nitrate: common themes and variations.  Abstract.  Author URL.

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Teaching

I am module leader for BIO1325 ‘Introduction to Biotechnology’ and lecture on various additional modules.

I am a Fellow of Higher Education Academy.

Modules

2022/23

Information not currently available


Supervision / Group

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