Studies by electron paramagnetic resonance spectroscopy of xanthine oxidase enriched with molybdenum-95 and with molybdenum-97

Biochemistry ◽  
1988 ◽  
Vol 27 (10) ◽  
pp. 3603-3609 ◽  
Author(s):  
Graham N. George ◽  
Robert C. Bray
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Xanthine Oxidase ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Resonance Spectroscopy ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

scholarly journals Electron-paramagnetic-resonance spectroscopy of complexes of xanthine oxidase with xanthine and uric acid

1978 ◽  
Vol 171 (3) ◽  
pp. 653-658 ◽  
Author(s):  
R C Bray ◽  
M J Barber ◽  
D J Lowe
Keyword(s):  
Electron Paramagnetic Resonance ◽  
Uric Acid ◽  
Xanthine Oxidase ◽  
Catalytic Reaction ◽  
Active Site ◽  
Electron Paramagnetic Resonance Spectroscopy ◽  
Resonance Spectroscopy ◽  
Substrate Molecule ◽  
Paramagnetic Resonance ◽  
Electron Paramagnetic

Molybdenum(V) e.p.r. signals from reduced functional milk xanthine oxidase molecules (the Rapid signals), obtained in the presence of purine substrates and products, were further investigated [cf. Bray & Vänngård, (1969) Biochem. J. 114, 725-734; Pick & Bray (1969) Biochem. J. 114, 735-742]. Xanthine forms two complexes with the enzyme that are believed to correspond to different orientations of the substrate molecule in the active site. Only one complex appears to undergo the catalytic reaction. Non-productive complexes, analogous to theone with xanthine, are not formed by 1-methylxanthine or purine. Uric acid forms more than one e.p.r.-detectable complex, one of which is analogous to the non-productive xanthine complex. The computer program used for handing the e.p.r. data is described briefly.

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