Studies by electron-paramagnetic-resonance spectroscopy and stopped-flow spectrophotometry on the mechanism of action of turkey liver xanthine dehydrogenase.
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A new non-functional form of milk xanthine oxidase containing stable quinquivalent molybdenum.Spectroscopic and electronic structure studies probing covalency contributions to C-H bond activation and transition-state stabilization in xanthine oxidase.Magnetic coupling of the molybdenum and iron-sulphur centres in xanthine oxidase and xanthine dehydrogenases.The inorganic biochemistry of molybdoenzymes.Studies by electron-paramagnetic-resonance spectroscopy on the mechanism of action of xanthine dehydrogenase from Veillonella alcalescens.Electron-paramagnetic-resonance studies on the molybdenum of nitrate reductase from Escherichia coli K12.Oxidation-reduction potentials of molybdenum, flavin and iron-sulphur centres in milk xanthine oxidase.Stopped-flow spectrophotometric studies on the reaction of turkey liver xanthine dehydrogenase with reducing substrates.Electron-paramagnetic-resonance spectroscopy of complexes of xanthine oxidase with xanthine and uric acid.The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase.The molybdenum centre of native xanthine oxidase. Evidence for proton transfer from substrates to the centre and for existence of an anion-binding site.Oxidation--reduction potentials of turkey liver xanthine dehydrogenase and the origins of oxidase and dehydrogenase behaviour in molybdenum-containing hydroxylases.Information from e.p.r. spectroscopy on the iron-sulphur centres of the iron-molybdenum protein (aldehyde oxidoreductase) of Desulfovibrio gigas.Rapid type 2 molybdenum(V) electron-paramagnetic resonance signals from xanthine oxidase and the structure of the active centre of the enzyme.Information from e.x.a.f.s. spectroscopy on the structures of different forms of molybdenum in xanthine oxidase and the catalytic mechanism of the enzyme.Studies by electron-paramagnetic-resonance spectroscopy of the molybdenum centre of aldehyde oxidase.Electron-paramagnetic-resonance parameters of molybdenum(V) in sulphite oxidase from chicken liver.Consequences of removal of a molybdenum ligand (DmsA-Ser-176) of Escherichia coli dimethyl sulfoxide reductase.
P2860
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P2860
Studies by electron-paramagnetic-resonance spectroscopy and stopped-flow spectrophotometry on the mechanism of action of turkey liver xanthine dehydrogenase.
description
1976 nî lūn-bûn
@nan
1976年の論文
@ja
1976年学术文章
@wuu
1976年学术文章
@zh-cn
1976年学术文章
@zh-hans
1976年学术文章
@zh-my
1976年学术文章
@zh-sg
1976年學術文章
@yue
1976年學術文章
@zh
1976年學術文章
@zh-hant
name
Studies by electron-paramagnet ...... liver xanthine dehydrogenase.
@en
Studies by electron-paramagnet ...... liver xanthine dehydrogenase.
@nl
type
label
Studies by electron-paramagnet ...... liver xanthine dehydrogenase.
@en
Studies by electron-paramagnet ...... liver xanthine dehydrogenase.
@nl
prefLabel
Studies by electron-paramagnet ...... liver xanthine dehydrogenase.
@en
Studies by electron-paramagnet ...... liver xanthine dehydrogenase.
@nl
P2093
P2860
P356
P1433
P1476
Studies by electron-paramagnet ...... liver xanthine dehydrogenase.
@en
P2093
P2860
P304
P356
10.1042/BJ1530297
P407
P577
1976-02-01T00:00:00Z