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Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibite...
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Zeitschriftentitel: | Biochemical Journal |
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Personen und Körperschaften: | , , , , |
In: | Biochemical Journal, 233, 1986, 1, S. 107-110 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
Portland Press Ltd.
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Schlagwörter: |
author_facet |
Peterson, J Godfrey, C Thomson, A J George, G N Bray, R C Peterson, J Godfrey, C Thomson, A J George, G N Bray, R C |
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author |
Peterson, J Godfrey, C Thomson, A J George, G N Bray, R C |
spellingShingle |
Peterson, J Godfrey, C Thomson, A J George, G N Bray, R C Biochemical Journal Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal Cell Biology Molecular Biology Biochemistry |
author_sort |
peterson, j |
spelling |
Peterson, J Godfrey, C Thomson, A J George, G N Bray, R C 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2330107 <jats:p>The magnetic circular-dichroism (m.c.d.) spectra in the temperature range 1.5-100 K and the electronic absorption spectra at 4.2 and 295 K were measured for a number of desulpho xanthine oxidase derivatives. There were no significant differences between the absorption spectra that could be attributed to molybdenum. However, the visible-region m.c.d. spectrum of the ethanediol-treated metalloprotein (which gives rise to the Desulpho Inhibited e.p.r. signal) contained features assignable to Mo(V) absorption bands. This is the first report of the detection of optical bands of Mo(V) in an enzyme in the presence of other chromophoric centres.</jats:p> Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal Biochemical Journal |
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10.1042/bj2330107 |
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Portland Press Ltd., 1986 |
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Portland Press Ltd., 1986 |
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0264-6021 1470-8728 |
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1986 |
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Portland Press Ltd. |
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Biochemical Journal |
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title |
Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_unstemmed |
Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_full |
Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_fullStr |
Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_full_unstemmed |
Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_short |
Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_sort |
detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (v) in the form of xanthine oxidase giving the desulpho inhibited e.p.r. signal |
topic |
Cell Biology Molecular Biology Biochemistry |
url |
http://dx.doi.org/10.1042/bj2330107 |
publishDate |
1986 |
physical |
107-110 |
description |
<jats:p>The magnetic circular-dichroism (m.c.d.) spectra in the temperature range 1.5-100 K and the electronic absorption spectra at 4.2 and 295 K were measured for a number of desulpho xanthine oxidase derivatives. There were no significant differences between the absorption spectra that could be attributed to molybdenum. However, the visible-region m.c.d. spectrum of the ethanediol-treated metalloprotein (which gives rise to the Desulpho Inhibited e.p.r. signal) contained features assignable to Mo(V) absorption bands. This is the first report of the detection of optical bands of Mo(V) in an enzyme in the presence of other chromophoric centres.</jats:p> |
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author | Peterson, J, Godfrey, C, Thomson, A J, George, G N, Bray, R C |
author_facet | Peterson, J, Godfrey, C, Thomson, A J, George, G N, Bray, R C, Peterson, J, Godfrey, C, Thomson, A J, George, G N, Bray, R C |
author_sort | peterson, j |
container_issue | 1 |
container_start_page | 107 |
container_title | Biochemical Journal |
container_volume | 233 |
description | <jats:p>The magnetic circular-dichroism (m.c.d.) spectra in the temperature range 1.5-100 K and the electronic absorption spectra at 4.2 and 295 K were measured for a number of desulpho xanthine oxidase derivatives. There were no significant differences between the absorption spectra that could be attributed to molybdenum. However, the visible-region m.c.d. spectrum of the ethanediol-treated metalloprotein (which gives rise to the Desulpho Inhibited e.p.r. signal) contained features assignable to Mo(V) absorption bands. This is the first report of the detection of optical bands of Mo(V) in an enzyme in the presence of other chromophoric centres.</jats:p> |
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id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajIzMzAxMDc |
imprint | Portland Press Ltd., 1986 |
imprint_str_mv | Portland Press Ltd., 1986 |
institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14 |
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mega_collection | Portland Press Ltd. (CrossRef) |
physical | 107-110 |
publishDate | 1986 |
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publisher | Portland Press Ltd. |
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series | Biochemical Journal |
source_id | 49 |
spelling | Peterson, J Godfrey, C Thomson, A J George, G N Bray, R C 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2330107 <jats:p>The magnetic circular-dichroism (m.c.d.) spectra in the temperature range 1.5-100 K and the electronic absorption spectra at 4.2 and 295 K were measured for a number of desulpho xanthine oxidase derivatives. There were no significant differences between the absorption spectra that could be attributed to molybdenum. However, the visible-region m.c.d. spectrum of the ethanediol-treated metalloprotein (which gives rise to the Desulpho Inhibited e.p.r. signal) contained features assignable to Mo(V) absorption bands. This is the first report of the detection of optical bands of Mo(V) in an enzyme in the presence of other chromophoric centres.</jats:p> Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal Biochemical Journal |
spellingShingle | Peterson, J, Godfrey, C, Thomson, A J, George, G N, Bray, R C, Biochemical Journal, Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal, Cell Biology, Molecular Biology, Biochemistry |
title | Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_full | Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_fullStr | Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_full_unstemmed | Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_short | Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
title_sort | detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (v) in the form of xanthine oxidase giving the desulpho inhibited e.p.r. signal |
title_unstemmed | Detection by low-temperature magnetic circular-dichroism spectroscopy of optical absorption bands due to molybdenum (V) in the form of xanthine oxidase giving the Desulpho Inhibited e.p.r. signal |
topic | Cell Biology, Molecular Biology, Biochemistry |
url | http://dx.doi.org/10.1042/bj2330107 |