@article{fdi:010051885,
  title = {{B}iochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from {D}esulfovibrio aminophilus},
  author = {{T}happer, {A}. and {R}ivas, {M}.{G}. and {B}rondino, {C}.{D}. and {O}llivier, {B}ernard and {F}auque, {G}uy and {M}oura, {I}. and {M}oura, {J}. {J}. {G}.},
  editor = {},
  language = {{ENG}},
  abstract = {{A}ldehyde oxidoreductase ({AOR}) activity has been found in a number of sulfate-reducing bacteria. {T}he enzyme that is responsible for the conversion of aldehydes to carboxylic acids is a mononuclear molybdenum enzyme belonging to the xanthine oxidase family. {W}e report here the purification and characterization of {AOR} isolated from the sulfate-reducing bacterium {D}esulfovibrio ({D}.) aminophilus {DSM} 12254, an aminolytic strain performing thiosulfate dismutation. {T}he enzyme is a homodimer (ca. 200 k{D}a), containing a molybdenum centre and two [2{F}e-2{S}] clusters per monomer. {UV}/{V}isible and electron paramagnetic resonance ({EPR}) spectra of {D}. aminophilus {AOR} recorded in as-prepared and reduced states are similar to those obtained in {AOR}s from {D}esulfovibrio gigas, {D}esulfovibrio desulfuricans and {D}esulfovibrio alaskensis. {D}espite {AOR} from {D}. aminophilus is closely related to other {AOR}s, it presents lower activity towards aldehydes and no activity towards {N}-heterocyclic compounds, which suggests another possible role for this enzyme in vivo. {A} comparison of the molecular and {EPR} properties of {AOR}s from different {D}esulfovibrio species is also included. ({C}) 2005 {E}lsevier {I}nc. {A}ll rights reserved.},
  keywords = {aldehyde oxidoreductase ; {D}esulfovibrio aminophilus ; mononuclear molybdenum enzymes ; xanthine oxidase family ; sulfate reducing bacteria},
  booktitle = {},
  journal = {{J}ournal of {I}norganic {B}iochemistry},
  volume = {100},
  numero = {1},
  pages = {44--50},
  ISSN = {0162-0134},
  year = {2006},
  DOI = {10.1016/j.jinorgbio.2005.09.013},
  URL = {https://www.documentation.ird.fr/hor/fdi:010051885},
}