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 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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publishDateSort 1986
publisher Portland Press Ltd.
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series Biochemical Journal
source_id 49
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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match_str peterson1986detectionbylowtemperaturemagneticcirculardichroismspectroscopyofopticalabsorptionbandsduetomolybdenumvintheformofxanthineoxidasegivingthedesulphoinhibitedeprsignal
mega_collection Portland Press Ltd. (CrossRef)
physical 107-110
publishDate 1986
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publisher Portland Press Ltd.
record_format ai
recordtype ai
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