• search hit 1 of 1
Back to Result List

Pyranopterin dithiolene distortions relevant to electron transfer in xanthine oxidase/dehydrogenase

  • The reducing substrates 4-thiolumazine and 2,4-dithiolumazine have been used to form Mo-IV-product complexes with xanthine oxidase (XO) and xanthine dehydrogenase. These Mo-IV-product complexes display an intense metal-to-ligand charge-transfer (MLCT) band in the near-infrared region of the spectrum. Optical pumping into this MLCT band yields resonance Raman spectra of the Mo site that are devoid of contributions from the highly absorbing FAD and 2Fe2S clusters in the protein. The resonance Raman spectra reveal in-plane bending modes of the bound product and low-frequency molybdenum dithiolene and pyranopterin dithiolene vibrational modes. This work provides keen insight into the role of the pyranopterin dithiolene in electron-transfer reactivity.

Export metadata

Additional Services

Search Google Scholar Statistics
Metadaten
Author details:Chao Dong, Jing Yang, Silke Lehnkuehler, Martin L. Kirk
DOI:https://doi.org/10.1021/ic500873y
ISSN:0020-1669
ISSN:1520-510X
Pubmed ID:https://pubmed.ncbi.nlm.nih.gov/24979205
Title of parent work (English):Inorganic chemistry
Publisher:American Chemical Society
Place of publishing:Washington
Publication type:Article
Language:English
Year of first publication:2014
Publication year:2014
Release date:2017/03/27
Volume:53
Issue:14
Number of pages:3
First page:7077
Last Page:7079
Funding institution:National Institutes of Health [GM 057378]
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer review:Referiert
Accept ✔
This website uses technically necessary session cookies. By continuing to use the website, you agree to this. You can find our privacy policy here.