EPR studies of the Mo-enzyme aldehyde oxidoreductase from Desulfovibrio gigas: An application of the Bloch-Wangsness-Redfield theory to a system containing weakly-coupled paramagnetic redox centers with different relaxation rates

Journal of Inorganic Biochemistry

Volumn 103, Issue 10, 2009, Pages 1342-1346

  González, Pablo J ^a   Barrera, Guillermo I ^b   Rizzi, Alberto C ^b   Moura, José J G ^a   Passeggi, Mario C G ^b   Brondino, Carlos D ^b  

^a DEPARTAMENTO DE QUÍMICA   (Portugal)

^b UNIVERSIDAD NACIONAL DEL LITORAL   (Argentina)

Author keywords

Aldehyde oxidoreductase; Electron paramagnetic resonance; Magnetic interactions; Molybdenum containing enzymes; Relaxation rate

Indexed keywords

ALDEHYDE DEHYDROGENASE; CARRIER PROTEIN; MOLYBDENUM; OXIDOREDUCTASE;

ARTICLE; CHEMICAL INTERACTION; CONTROLLED STUDY; DESULFOVIBRIO GIGAS; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; HIGH TEMPERATURE; LOW TEMPERATURE; MATHEMATICAL ANALYSIS; NONHUMAN; OXIDATION REDUCTION REACTION; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE; THEORETICAL MODEL;

ALDEHYDE REDUCTASE; BACTERIAL PROTEINS; DESULFOVIBRIO GIGAS; ELECTRON SPIN RESONANCE SPECTROSCOPY; MOLYBDENUM;

DESULFOVIBRIO GIGAS;

EID: 70349506051     PISSN: 01620134     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jinorgbio.2009.06.006     Document Type: Article

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