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Resonance Raman studies of the flavin and iron-sulfur centers of milk xanthine oxidase.
Biochemistry. 1985 May 21; 24(11):2768-72.B

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.

Authors

No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

3839680

Citation

Willis, L J., and T M. Loehr. "Resonance Raman Studies of the Flavin and Iron-sulfur Centers of Milk Xanthine Oxidase." Biochemistry, vol. 24, no. 11, 1985, pp. 2768-72.
Willis LJ, Loehr TM. Resonance Raman studies of the flavin and iron-sulfur centers of milk xanthine oxidase. Biochemistry. 1985;24(11):2768-72.
Willis, L. J., & Loehr, T. M. (1985). Resonance Raman studies of the flavin and iron-sulfur centers of milk xanthine oxidase. Biochemistry, 24(11), 2768-72.
Willis LJ, Loehr TM. Resonance Raman Studies of the Flavin and Iron-sulfur Centers of Milk Xanthine Oxidase. Biochemistry. 1985 May 21;24(11):2768-72. PubMed PMID: 3839680.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Resonance Raman studies of the flavin and iron-sulfur centers of milk xanthine oxidase. AU - Willis,L J, AU - Loehr,T M, PY - 1985/5/21/pubmed PY - 1985/5/21/medline PY - 1985/5/21/entrez SP - 2768 EP - 72 JF - Biochemistry JO - Biochemistry VL - 24 IS - 11 N2 - 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. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/3839680/Resonance_Raman_studies_of_the_flavin_and_iron_sulfur_centers_of_milk_xanthine_oxidase_ L2 - https://antibodies.cancer.gov/detail/CPTC-BRCA2-1 DB - PRIME DP - Unbound Medicine ER -