Gn. George et al., X-RAY-ABSORPTION SPECTROSCOPY OF THE MOLYBDENUM SITE OF ESCHERICHIA-COLI FORMATE DEHYDROGENASE, Journal of the American Chemical Society, 120(6), 1998, pp. 1267-1273
X-ray absorption spectroscopy at the molybdenum and selenium K-edges h
as been used to probe the active site structure of Escherichia coli fo
rmate dehydrogenase H. The active sites of both oxidized and reduced w
ild-type protein, and of a variant containing cysteine instead of sele
nocysteine, were studied. The oxidized and reduced enzymes were found
to be very similar, both containing a novel des-oxo molybdenum site, w
ith four Mo-S ligands at 2.35 Angstrom, (probably) one Mo-O at 2.1 Ang
strom, and one Mo-Se ligand at 2.62 Angstrom being indicated from the
Mo K-edge data. The selenium K-edge EXAFS not only is in good agreemen
t with the Mo K-edge data but also indicates the unexpected presence o
f Se-S ligation, with a bond length of 2.19 Angstrom. We suggest that
the active site of Escherichia coli formate dehydrogenase H contains a
novel selenosulfide ligand to molybdenum, where the selenium and sulf
ur originate from selenocysteine and one of the pterin-cofactor dithio
lenes, respectively.