title: Resonance Raman study on the iron-sulfur centers of Desulfovibrio gigas aldehyde oxidoreductase.
abstract: Resonance Raman spectra of the molybdenum containing aldehyde oxidoreductase from Desulfovibrio gigas were recorded at liquid nitrogen temperature with various excitation wavelengths. The spectra indicate that all the iron atoms are organised in [2Fe-2S] type centers consistent with cysteine ligations. No vibrational modes involving molybdenum could be clearly identified. The features between 280 and 420 cm-1 are similar but different from those of typical plant ferredoxin-like [2Fe-2S] cluster. The data are consistent with the presence of a plant ferredoxin-like cluster (center I) and a unique [2Fe-2S] cluster (center II), as suggested by other spectroscopic studies. The Raman features of center II are different from those of other [2Fe-2S] clusters in proteins. In addition, a strong peak at ca. 683 cm-1, which is not present in other [2Fe-2S] clusters in proteins, was observed with purple excitation (406.7-413.1 nm). The peak is assigned to enhanced cysteinyl C-S stretching in center II, suggesting a novel geometry for this center.
authors.affiliation: Department of Physics, Emory University, Atlanta, GA 30322, USA.
authors.forename: V
authors.initials: V
authors.lastname: Zhelyaskov
authors.forename: K T
authors.initials: KT
authors.lastname: Yue
authors.forename: J
authors.initials: J
authors.lastname: LeGall
authors.forename: B A
authors.initials: BA
authors.lastname: Barata
authors.forename: J J
authors.initials: JJ
authors.lastname: Moura
mesh_terms: D000445:Aldehyde Oxidoreductases / Q000737:chemistry*; D003901:Desulfovibrio / Q000201:enzymology*; D007506:Iron-Sulfur Proteins / Q000032:analysis*; D008982:Molybdenum; D010944:Plants / Q000201:enzymology; D013059:Spectrum Analysis, Raman
chemical_list: D007506:Iron-Sulfur Proteins; D008982:Molybdenum; D000445:Aldehyde Oxidoreductases