| Literature DB >> 12206891 |
Sean J Elliott1, Christophe Léger, Harsh R Pershad, Judy Hirst, Kerensa Heffron, Nicolas Ginet, Francis Blasco, Richard A Rothery, Joel H Weiner, Fraser A Armstrong.
Abstract
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.Mesh:
Substances:
Year: 2002 PMID: 12206891 DOI: 10.1016/s0005-2728(02)00254-2
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002