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SOX  -  sulfite oxidase

Arabidopsis thaliana

Synonyms: AT-SO, AtSO, F28J7.38, F28J7_38, SULFITE OXIDASE
 
 
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Disease relevance of SOX

 

High impact information on SOX

 

Biological context of SOX

  • In contrast to homologous animal enzymes, At-SO lacks the heme domain, which is evident both from the amino acid sequence and from its enzymological and spectral properties [4].
  • It is proposed that, depending on the conformation of Arg374, the active site of At-SO may be in "closed" or "open" forms that differ in the degree of accessibility of the Mo center to substrate and water molecules [5].
 

Anatomical context of SOX

  • Sulfite oxidase from T. thermophilus, purified to homogeneity, is a monomeric enzyme with an apparent molecular mass of 39.1 kDa and is almost exclusively located in the periplasm fraction [3].
 

Associations of SOX with chemical compounds

  • In mammals and birds, sulfite oxidase (SO) is a homodimeric molybdenum enzyme consisting of an N-terminal heme domain and a C-terminal molybdenum domain (EC ) [4].
  • Reduction of At-SO with sulfite at high pH generates the well-known high-pH (hpH) signal common to all sulfite oxidizing enzymes [5].
  • It is suggested that at low pH the sulfite-reduced At-SO has coordinated sulfate and is in the "closed form". Reoxidation to Mo(V) by ferricyanide leaves bound sulfate trapped at the active site, and consequently, there are no ligands with exchangeable protons [5].
  • On the other hand, reduction of At-SO with Ti(III) citrate at pH 6 generates a Mo(V) signal with large hyperfine splittings from a single exchangeable proton, as is typically observed for lpH SO from vertebrates [5].
  • The Arabidopsis AtMCP and rice OsMCP genes which encode proteins highly homologous to molybdoenzymes of the sulphite oxidase family were isolated and characterized [6].

References

  1. Characterization and metabolic function of a peroxisomal sarcosine and pipecolate oxidase from Arabidopsis. Goyer, A., Johnson, T.L., Olsen, L.J., Collakova, E., Shachar-Hill, Y., Rhodes, D., Hanson, A.D. J. Biol. Chem. (2004) [Pubmed]
  2. Identification and characterization of a novel bacterial sulfite oxidase with no heme binding domain from Deinococcus radiodurans. D'Errico, G., Di Salle, A., La Cara, F., Rossi, M., Cannio, R. J. Bacteriol. (2006) [Pubmed]
  3. A novel thermostable sulfite oxidase from Thermus thermophilus: characterization of the enzyme, gene cloning and expression in Escherichia coli. Di Salle, A., D'Errico, G., La Cara, F., Cannio, R., Rossi, M. Extremophiles (2006) [Pubmed]
  4. Identification and biochemical characterization of Arabidopsis thaliana sulfite oxidase. A new player in plant sulfur metabolism. Eilers, T., Schwarz, G., Brinkmann, H., Witt, C., Richter, T., Nieder, J., Koch, B., Hille, R., Hänsch, R., Mendel, R.R. J. Biol. Chem. (2001) [Pubmed]
  5. Structures of the Mo(V) forms of sulfite oxidase from Arabidopsis thaliana by pulsed EPR spectroscopy. Astashkin, A.V., Hood, B.L., Feng, C., Hille, R., Mendel, R.R., Raitsimring, A.M., Enemark, J.H. Biochemistry (2005) [Pubmed]
  6. Molecular cloning and characterization of plant genes encoding novel peroxisomal molybdoenzymes of the sulphite oxidase family. Nakamura, T., Meyer, C., Sano, H. J. Exp. Bot. (2002) [Pubmed]
 
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