Abstract
X-ray absorption spectroscopy at the molybdenum and selenium K-edges has been used to probe the active site structure of Escherichia coli formate dehydrogenase H. The active sites of both oxidized and reduced wild-type protein, and of a variant containing cysteine instead of selenocysteine, were studied. The oxidized and reduced enzymes were found to be very similar, both containing a novel des-oxo molybdenum site, with four Mo−S ligands at 2.35 A, (probably) one Mo−O at 2.1 A, and one Mo−Se ligand at 2.62 A being indicated from the Mo K-edge data. The selenium K-edge EXAFS not only is in good agreement with the Mo K-edge data but also indicates the unexpected presence of Se−S ligation, with a bond length of 2.19 A. We suggest that the active site of Escherichia coli formate dehydrogenase H contains a novel seleno-sulfide ligand to molybdenum, where the selenium and sulfur originate from selenocysteine and one of the pterin-cofactor dithiolenes, respectively.
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