Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 75, Issue 9, Pages 1662-1667Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.110153
Keywords
formate oxidase; 8-formyl-FAD; oxidation-reduction potential; crystallographic structure; His-Arg pair
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Formate oxidase of Aspergillus oryzae RIB40 contains an 8-replaced FAD with molecular mass of 799 as cofactor. The H-1-NMR spectrum of the cofactor fraction obtained from the enzyme indicated that the 8-replaced FAD in the fraction was 8-formyl-FAD, present in open form and hemiacetal form. The oxidation-reduction potentials of the open and hemiacetal forms were estimated by cyclic voltammetry to be -47 and -177 mV vs. Normal Hydrogen Electrode respectively. The structure of the enzyme was constructed using diffraction data to 2.24 angstrom resolution collected from a crystal of the enzyme. His(511) and Arg(554) were situated close to the pyrimidine part of the isoalloxazine ring of 8-formyl-FAD in open form. The enzyme had 8-formyl-FAD, the oxidation potential of which was approximately 160 mV more positive than that of FAD, and the His-Arg pair at the catalytic site, unlike the other enzymes belonging to the glucose-methanol-choline oxidoreductase family.
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