Berzelius stated that catalysts remain unaltered in their reaction environment. However,
catalyst deactivation always becomes noticeable at certain timescales, frequently hindering …

The reaction takes place at a specialized metal center that dramatically increases the acidity
of H2 and leads to a heterolytic splitting of the molecule which is strongly accelerated by the …

The [FeFe]-hydrogenase catalytic site H cluster is a complex iron sulfur cofactor that is
sensitive to oxygen (O2). The O2 sensitivity is a significant barrier for production of hydrogen …

FeFe hydrogenases are the most efficient H2-producing enzymes. However, inactivation by
O2 remains an obstacle that prevents them being used in many biotechnological devices …

Clostridia comprise bacteria of environmental, biotechnological and medical interest and
many commensals of the gut microbiota. Because of their strictly anaerobic lifestyle, oxygen …

The instability of [FeFe]-H2ases and their biomimetics toward O2 renders them inefficient to
implement in practical H2 generation (HER). Previous investigations on synthetic models as …

Hydrogenases are metalloproteins capable of catalyzing the interconversion between
molecular hydrogen and protons and electrons. The iron–sulfur clusters within the enzyme …

Natural and most artificial photosynthesis systems utilize a pair of light absorbers to convert
CO 2 into sugar and fuels. However, much of the solar energy is lost as unabsorbed (mainly …

The mechanism of reaction of FeFe hydrogenases with oxygen has been debated. It is
complex, apparently very dependent on the details of the protein structure, and difficult to …

Hydrogenases catalyze the reduction of protons and oxidation of molecular hydrogen with
high turnover frequencies and low overpotentials under ambient conditions. The …