Lista de obras -

A threonine stabilizes the NiC and NiR catalytic intermediates of [NiFe]-hydrogenase.

artículo científico publicado en 2015

Access to the Active Site of Periplasmic Nitrate Reductase: Insights from Site-Directed Mutagenesis and Zinc Inhibition Studies†

artículo científico publicado en 2007

Changing the Ligation of the Distal [4Fe4S] Cluster in NiFe Hydrogenase Impairs Inter- and Intramolecular Electron Transfers

scientific article published on 01 April 2006

Correcting for Electrocatalyst Desorption and Inactivation in Chronoamperometry Experiments

scientific article published on 01 April 2009

Crystallographic studies of [NiFe]-hydrogenase mutants: towards consensus structures for the elusive unready oxidized states

artículo científico publicado en 2015

Dependence of catalytic activity on driving force in solution assays and protein film voltammetry: insights from the comparison of nitrate reductase mutants

artículo científico publicado en 2010

Effects of slow substrate binding and release in redox enzymes: theory and application to periplasmic nitrate reductase

artículo científico publicado en 2007

Introduction of methionines in the gas channel makes [NiFe] hydrogenase aero-tolerant

artículo científico publicado en 2009

Major Mo(V) EPR signature of Rhodobacter sphaeroides periplasmic nitrate reductase arising from a dead-end species that activates upon reduction. Relation to other molybdoenzymes from the DMSO reductase family

artículo científico publicado en 2008

O2-independent formation of the inactive states of NiFe hydrogenase

scientific article published on 11 November 2012

Original Design of an Oxygen-Tolerant [NiFe] Hydrogenase: Major Effect of a Valine-to-Cysteine Mutation near the Active Site

artículo científico publicado en 2010

Rates of Intra- and Intermolecular Electron Transfers in Hydrogenase Deduced from Steady-State Activity Measurements

artículo científico publicado en 2011

Relating diffusion along the substrate tunnel and oxygen sensitivity in hydrogenase.