Abstract：
:The metal-free hydrogenase from methanogenic archaea (Hmd) is a unique enzyme: it catalyzes the reaction of its substrate, methenyl-tetrahydromethanopterin, with molecular hydrogen without the aid of a transition metal. In other words, Hmd is currently the only example of a purely organic hydrogenation catalyst. Recent results from various fields have shed new light on this enzyme. In biochemistry, there is experimental proof that a tightly bound (and metal-free) cofactor exists. Ab initio calculations have revealed that the concerted action of the Lewis-acidic substrate and a Brønsted-base appears to induce facile heterolysis of the hydrogen molecule. In chemical model studies, a transition-metal-free hydrogenation of ketones was achieved in the presence of catalytic base. Taken together, the experimental results available to date point to an enzymatic mechanism in which the hydrogen molecule is heterolyzed by the joint action of the Lewis-acidic substrate methenyl-tetrahydromethanopterin and a Brønsted-base in the active site (i.e. by bifunctional catalysis).
journal_name
Curr Opin Chem Bioljournal_title
Current opinion in chemical biologyauthors
Berkessel Adoi
10.1016/s1367-5931(00)00245-3subject
Has Abstractpub_date
2001-10-01 00:00:00pages
486-90issue
5eissn
1367-5931issn
1879-0402pii
S1367-5931(00)00245-3journal_volume
5pub_type
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