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Title: Vanadium K-edge X-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum

Abstract

Bromoperoxidase from Ascophyllum nodusum was the first vanadium-containing enzyme to be isolated. X-ray absorption spectra have now been collected in order to investigate the coordination of vanadium in the native, native plus bromide, native plus hydrogen peroxide, and dithionite-reduced forms of the enzyme. The edge and X-ray absorption near-edge structures show that, in the four samples studied, it is only on reduction of the native enzyme that the metal site is substantially altered. In addition, these data are consistent with the presence of vanadium(IV) in the reduced enzyme and vanadium(V) in the other samples. Extended X-ray absorption fine structure data confirm that there are structural changes at the metal site on reduction of the native enzyme, notably a lengthening of the average inner-shell distance, and the presence of terminal oxygen together with histidine and oxygen-donating residues.

Authors:
; ; ; ;  [1]
  1. (Univ. of Manchester (England))
Publication Date:
OSTI Identifier:
7192086
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemistry; (USA); Journal Volume: 28:19
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; PEROXIDASES; MOLECULAR STRUCTURE; ALGAE; SPECTROPHOTOMETRY; VANADIUM; X-RAY SPECTRA; ELEMENTS; ENZYMES; METALS; OXIDOREDUCTASES; PLANTS; SPECTRA; TRANSITION ELEMENTS; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Arber, J.M., de Boer, E., Garner, C.D., Hasnain, S.S., and Wever, R. Vanadium K-edge X-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum. United States: N. p., 1989. Web. doi:10.1021/bi00445a062.
Arber, J.M., de Boer, E., Garner, C.D., Hasnain, S.S., & Wever, R. Vanadium K-edge X-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum. United States. doi:10.1021/bi00445a062.
Arber, J.M., de Boer, E., Garner, C.D., Hasnain, S.S., and Wever, R. Tue . "Vanadium K-edge X-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum". United States. doi:10.1021/bi00445a062.
@article{osti_7192086,
title = {Vanadium K-edge X-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum},
author = {Arber, J.M. and de Boer, E. and Garner, C.D. and Hasnain, S.S. and Wever, R.},
abstractNote = {Bromoperoxidase from Ascophyllum nodusum was the first vanadium-containing enzyme to be isolated. X-ray absorption spectra have now been collected in order to investigate the coordination of vanadium in the native, native plus bromide, native plus hydrogen peroxide, and dithionite-reduced forms of the enzyme. The edge and X-ray absorption near-edge structures show that, in the four samples studied, it is only on reduction of the native enzyme that the metal site is substantially altered. In addition, these data are consistent with the presence of vanadium(IV) in the reduced enzyme and vanadium(V) in the other samples. Extended X-ray absorption fine structure data confirm that there are structural changes at the metal site on reduction of the native enzyme, notably a lengthening of the average inner-shell distance, and the presence of terminal oxygen together with histidine and oxygen-donating residues.},
doi = {10.1021/bi00445a062},
journal = {Biochemistry; (USA)},
number = ,
volume = 28:19,
place = {United States},
year = {Tue Sep 19 00:00:00 EDT 1989},
month = {Tue Sep 19 00:00:00 EDT 1989}
}