title: FTIR spectroscopy of metalloproteins.
abstract: Absorption of infrared radiation by proteins gives important information about their structure and function. The most intense infrared bands correspond to the overlap of all the peptide bond absorption. Additionally, in many metalloproteins their prosthetic groups have intrinsic ligands or bind substrates/inhibitors that absorb intensively in the infrared. Here, we describe thoroughly several Fourier transform infrared methods for studying structure-function relationships in metalloproteins, using hydrogenases as an example.
authors.affiliation: Laboratorio de Bioelectrocatalisis, Departamento de Biocatalisis, Instituto de Catalisis y Petroleoquimica, Madrid, Spain.
authors.forename: Oscar
authors.initials: O
authors.lastname: Gutiérrez-Sanz
authors.forename: Olaf
authors.initials: O
authors.lastname: Rüdiger
authors.forename: Antonio L
authors.initials: AL
authors.lastname: De Lacey
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology; D003901:Desulfovibrio / Q000201:enzymology; D006864:Hydrogenase / Q000378:metabolism; D055767:Immobilized Proteins / Q000378:metabolism; D008667:Metalloproteins / Q000032:analysis*; D043367:Ralstonia / Q000201:enzymology; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
chemical_list: D055767:Immobilized Proteins; D008667:Metalloproteins; D000255:Adenosine Triphosphate; D006864:Hydrogenase