Haloperoxidases: Their Properties and Their Use in Organic Synthesis
- 1 January 1992
- book chapter
- Published by Elsevier
Abstract
No abstract availableThis publication has 100 references indexed in Scilit:
- Some structural aspects of vanadium bromoperoxidase from Ascophyllum nodosumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- A comparison of different (vanadium) bromoperoxidases; the bromoperoxidase from Corallina pilulifera is also a vanadium enzymeBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1989
- The mechanism of myeloperoxidase-dependent chlorination of monochlorodimedonBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Vanadium K-edge absorption spectrum of bromoperoxidase from Ascophyllum nodosumBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- Crystallization and subunit structure of canine myeloperoxidaseJournal of Molecular Biology, 1987
- The bromoperoxidase from the red alga Ceramium rubrum also contains vanadium as a prosthetic groupBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Isolation and characterization of a novel nonheme chloroperoxidaseBiochemical and Biophysical Research Communications, 1987
- Vanadium(V) as an essential element for haloperoxidase activity in marine brown algae: purification and characterization of a vanadium(V)-containing bromoperoxidase from Laminaria saccharinaBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- Bromoperoxidase from Ascophyllum nodosum: a novel class of enzymes containing vanadium as a prosthetic group?Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- A new approach (cyano-transfer) for cyanogen bromide activation of Sepharose at neutral pH, which yields activated resins, free of interfering nitrogen derivativesBiochemical and Biophysical Research Communications, 1982