(MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE

KNUTTEL K, Müller A, REHDER D, VILTER H, WITTNEBEN V (1992)
FEBS LETTERS 302(1): 11-14.

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DOI
Autor*in
KNUTTEL, K; Müller, AchimUniBi ; REHDER, D; VILTER, H; WITTNEBEN, V
Einrichtung
Fakultät für Chemie
Abstract / Bemerkung
Vanadate-dependent peroxidase A.n.I, the main isoenzyme (M(r) = 100 kDa) from the seaweed, Ascophyllum nodosum, contains 2 V per enzyme molecule (as shown by ICP-MS metal analysis) after complete reconstitution with vanadate (V), possibly distributed in a 1:1 ratio between the surface and active site. VO2+ is only weakly associated to the surface of A.n.I. There is no transport channel for VO2+. The EPR spectrum of the reduced holoenzyme is anisotropic (axial) already at room temperature, with EPR parameters similar to those of VO2+ complexes of small model peptides such as Ala-His, Gly-Tyr, Gly-Ser, Gly-Glu, Ser-Gly and Phe-Glu. The complex formation between Ala-His and H2VO4-, in water has also been investigated (by V-51 NMR); the formation constant at pH 7.2 amounts to 266(28) M-1.
Stichworte
V-51 NUCLEAR; ELECTRON PARAMAGNETIC RESONANCE; VANADATE-PEPTIDE COMPLEX; VANADYL PEPTIDE COMPLEX; MAGNETIC RESONANCE SPECTROSCOPY; VANADATE-DEPENDENT PEROXIDASE
Erscheinungsjahr
1992
Zeitschriftentitel
FEBS LETTERS
Band
302
Ausgabe
1
Seite(n)
11-14
ISSN
0014-5793
Page URI
https://pub.uni-bielefeld.de/record/1648283

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KNUTTEL K, Müller A, REHDER D, VILTER H, WITTNEBEN V. (MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE. FEBS LETTERS. 1992;302(1):11-14.
KNUTTEL, K., Müller, A., REHDER, D., VILTER, H., & WITTNEBEN, V. (1992). (MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE. FEBS LETTERS, 302(1), 11-14. https://doi.org/10.1016/0014-5793(92)80272-I
KNUTTEL, K, Müller, Achim, REHDER, D, VILTER, H, and WITTNEBEN, V. 1992. “(MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE”. FEBS LETTERS 302 (1): 11-14.
KNUTTEL, K., Müller, A., REHDER, D., VILTER, H., and WITTNEBEN, V. (1992). (MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE. FEBS LETTERS 302, 11-14.
KNUTTEL, K., et al., 1992. (MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE. FEBS LETTERS, 302(1), p 11-14.
K. KNUTTEL, et al., “(MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE”, FEBS LETTERS, vol. 302, 1992, pp. 11-14.
KNUTTEL, K., Müller, A., REHDER, D., VILTER, H., WITTNEBEN, V.: (MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE. FEBS LETTERS. 302, 11-14 (1992).
KNUTTEL, K, Müller, Achim, REHDER, D, VILTER, H, and WITTNEBEN, V. “(MODEL) STUDIES ON VANADATE-DEPENDENT BROMO IODOPEROXIDASE FROM ASCOPHYLLUM-NODOSUM - VO(2+) IS NOT INCORPORATED INTO THE ACTIVE-SITE”. FEBS LETTERS 302.1 (1992): 11-14.

3 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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The trigonal-bipyramidal NO4 ligand set in biologically relevant vanadium compounds and their inorganic models.
Rehder D., J. Inorg. Biochem. 102(5-6), 2008
PMID: 18255153

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