Resonance Raman studies of the flavin and iron-sulfur centers of milk xanthine oxidase.

Abstract:

:Resonance Raman spectroscopy has been used to study milk xanthine oxidase, an enzyme containing molybdenum, binuclear iron-sulfur clusters, and FAD as cofactors. The contribution of FAD dominates the resonance Raman spectrum at frequencies above 500 cm-1. As expected, no bands assignable to FAD are observed in deflavo xanthine oxidase. The resonance Raman spectrum below 500 cm-1 reveals the contribution of the Fe2S2(Cys)4 groups with frequencies similar to those of adrenodoxin and putidaredoxin. Resonance enhancement profiles of the Fe2S2(Cys)4 clusters indicate intensity variations among the Fe2S2(Cys)4 peaks that are attributed to different excitation wavelength maxima of their bridging and terminal iron-sulfur vibrations. No evidence for Mo-ligand vibrations could be obtained by using excitation wavelengths between 363.8 and 514.5 nm.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Willis LJ,Loehr TM

doi

10.1021/bi00332a026

subject

Has Abstract

pub_date

1985-05-21 00:00:00

pages

2768-72

issue

11

eissn

0006-2960

issn

1520-4995

journal_volume

24

pub_type

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