Understanding and tuning the catalytic bias of hydrogenase. - Archive ouverte HAL Access content directly
Journal Articles Journal of the American Chemical Society Year : 2012

Understanding and tuning the catalytic bias of hydrogenase.

Abbas Abou Hamdan
  • Function : Author
Sébastien Dementin
Oscar Gutierrez-Sanz
  • Function : Author
Antonio de Lacey
  • Function : Author
Marc Rousset
  • Function : Author
Patrick Bertrand
  • Function : Author
Laurent Cournac
Christophe Léger


When enzymes are optimized for biotechnological purposes, the goal often is to increase stability or catalytic efficiency. However, many enzymes reversibly convert their substrate and product, and if one is interested in catalysis in only one direction, it may be necessary to prevent the reverse reaction. In other cases, reversibility may be advantageous because only an enzyme that can operate in both directions can turnover at a high rate even under conditions of low thermodynamic driving force. Therefore, understanding the basic mechanisms of reversibility in complex enzymes should help the rational engineering of these proteins. Here, we focus on NiFe hydrogenase, an enzyme that catalyzes H(2) oxidation and production, and we elucidate the mechanism that governs the catalytic bias (the ratio of maximal rates in the two directions). Unexpectedly, we found that this bias is not mainly determined by redox properties of the active site, but rather by steps which occur on sites of the proteins that are remote from the active site. We evidence a novel strategy for tuning the catalytic bias of an oxidoreductase, which consists in modulating the rate of a step that is limiting only in one direction of the reaction, without modifying the properties of the active site.
No file

Dates and versions

hal-00748324 , version 1 (05-11-2012)



Abbas Abou Hamdan, Sébastien Dementin, Pierre-Pol Liebgott, Oscar Gutierrez-Sanz, Pierre Richaud, et al.. Understanding and tuning the catalytic bias of hydrogenase.. Journal of the American Chemical Society, 2012, 134 (20), pp.8368-71. ⟨10.1021/ja301802r⟩. ⟨hal-00748324⟩
179 View
0 Download



Gmail Facebook Twitter LinkedIn More