| Literature DB >> 12459907 |
Antonio L DeLacey1, Victor M Fernandez, Marc Rousset, Christine Cavazza, E Claude Hatchikian.
Abstract
Site-directed mutagenesis of amino acid residues proximate to the active site of the Ni-Fe hydrogenase of Desulfovibrio fructosovorans has been done. The different mutants have been analyzed by FTIR spectroscopy and compared with wild type enzyme. The changes observed in the spectra confirm that hydrogen bonds between the CN(-) ligands of the active site's Fe atom and certain neighbor amino acid residues stabilize the active center within the protein matrix. However, kinetic analysis of the mutants indicates that none of the replaced residues have an important role in the catalytic mechanism of the hydrogenase.Entities:
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Year: 2002 PMID: 12459907 DOI: 10.1007/s00775-002-0397-4
Source DB: PubMed Journal: J Biol Inorg Chem ISSN: 0949-8257 Impact factor: 3.358