TY - JOUR
T1 - Biochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from Desulfovibrio aminophilus
AU - Thapper, Anders
AU - Rivas, Maria G.
AU - Brondino, Carlos D.
AU - Ollivier, Bernard
AU - Fauque, Guy
AU - Moura, Isabel
AU - Moura, José J. G.
N1 - M.G.R. thank Fundação para a Ciência e Tecnologia (Grants SFRP/BPD/5689/2001 and SFRH/BD/10784/2002, respectively, supported by the European Social Funding within the III Communitarian Support Board). C.D.B. and J.J.G.M. thank SECYT (Argentina) and GRICES (Portugal) by a bilateral collaborative grant. Work supported by Projects EC HPRN-CT-1999-00084, POCTI/1999/BME/35078, and POCTI/1999/BME/36152 in Portugal, and SEPCyT:PICT 2003-06-13872, CONICET PIP 02559/2000 and CAI+D-UNL in Argentina.
PY - 2006/1/1
Y1 - 2006/1/1
N2 - Aldehyde oxidoreductase (AOR) activity has been found in a number of sulfate-reducing bacteria. The enzyme that is responsible for the conversion of aldehydes to carboxylic acids is a mononuclear molybdenum enzyme belonging to the xanthine oxidase family. We report here the purification and characterization of AOR isolated from the sulfate-reducing bacterium Desulfovibrio (D.) aminophilus DSM 12254, an aminolytic strain performing thiosulfate dismutation. The enzyme is a homodimer (ca. 200 kDa), containing a molybdenum centre and two [2Fe-2S] clusters per monomer. UV/Visible and electron paramagnetic resonance (EPR) spectra of D. aminophilus AOR recorded in as-prepared and reduced states are similar to those obtained in AORs from Desulfovibrio gigas, Desulfovibrio desulfuricans and Desulfovibrio alaskensis. Despite AOR from D. aminophilus is closely related to other AORs, 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 AORs from different Desulfovibrio species is also included.
AB - Aldehyde oxidoreductase (AOR) activity has been found in a number of sulfate-reducing bacteria. The enzyme that is responsible for the conversion of aldehydes to carboxylic acids is a mononuclear molybdenum enzyme belonging to the xanthine oxidase family. We report here the purification and characterization of AOR isolated from the sulfate-reducing bacterium Desulfovibrio (D.) aminophilus DSM 12254, an aminolytic strain performing thiosulfate dismutation. The enzyme is a homodimer (ca. 200 kDa), containing a molybdenum centre and two [2Fe-2S] clusters per monomer. UV/Visible and electron paramagnetic resonance (EPR) spectra of D. aminophilus AOR recorded in as-prepared and reduced states are similar to those obtained in AORs from Desulfovibrio gigas, Desulfovibrio desulfuricans and Desulfovibrio alaskensis. Despite AOR from D. aminophilus is closely related to other AORs, 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 AORs from different Desulfovibrio species is also included.
KW - Aldehyde oxidoreductase
KW - Desulfovibrio aminophilus
KW - Mononuclear molybdenum enzymes
KW - Sulfate-reducing bacteria
KW - Xanthine oxidase family
UR - http://www.scopus.com/inward/record.url?scp=29344459603&partnerID=8YFLogxK
U2 - 10.1016/j.jinorgbio.2005.09.013
DO - 10.1016/j.jinorgbio.2005.09.013
M3 - Article
C2 - 16290059
AN - SCOPUS:29344459603
SN - 0162-0134
VL - 100
SP - 44
EP - 50
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
IS - 1
ER -