Organometallic iron: the key to biological hydrogen metabolism.
X-ray crystallography of iron-hydrogenases reveals that the active-site H-cluster contains an unmistakably organometallic dinuclear iron subcluster. The nickel-hydrogenases, which in general play different metabolic roles, have a distinct but related active-site structure. The new structural definition, combined with chemical analogs and theoretical treatment, points toward mechanistic understanding of iron-hydrogenases and the possibility of a unified mechanism for all hydrogenases.
Adams
M W
MW
Department of Biochemistry and Molecular Biology, University of Georgia, Athens 30602, USA. adams@bmb.uga.edu
Stiefel
E I
EI
D005290:Ferric Compounds / Q000737:chemistry* / Q000378:metabolism*; D006859:Hydrogen / Q000378:metabolism*; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D008956:Models, Chemical
D005290:Ferric Compounds; D006859:Hydrogen; C043296:nickel-iron hydrogenase; D006864:Hydrogenase