Detection and interpretation of redox potential optima in the catalytic activity of enzymes.

Journal article

It is no surprise that the catalytic activity of electron-transport enzymes may be optimised at certain electrochemical potentials in ways that are analogous to observations of pH-rate optima. This property is observed clearly in experiments in which an enzyme is adsorbed on an electrode surface which can supply or receive electrons rapidly and in a highly controlled manner. In such a way, the rate of catalysis can be measured accurately as a function of the potential (driving force) that is applied. In this paper, we draw attention to a few examples in which this property has been observed in enzymes that are associated with membrane-bound respiratory chains, and we discuss its possible origins and implications for in vivo regulation.

Authors: Elliott, S; Léger, C; Pershad, H; Hirst, J; Heffron, K

• Publication status: Published
• Journal: Biochimica et biophysica acta
• Volume: 1555
• Issue: 1-3
• Pages: 54-59
• Publication date: 2002-09-01
• DOI: 10.1016/s0005-2728(02)00254-2
• ISSN: 0006-3002
• Language: English
• Keywords: Hydrogen-Ion Concentration; Iron-Sulfur Proteins; Catalysis; Oxidation-Reduction; Escherichia coli; Mitochondria; Electrochemistry; Nitrate Reductase; Cattle; Animals; Nitrate Reductases; Electron Transport; Succinate Dehydrogenase; Oxidoreductases