Structural Studies of the Molybdenum Center of the Pathogenic R160Q Mutant of Human Sulfite Oxidase by Pulsed EPR Spectroscopy and (17)O and (33)S Labeling

Electron paramagnetic resonance (EPR) investigation of the Mo(V) center of the pathogenic R160Q mutant of human sulfite oxidase (hSO) confirms the presence of three distinct species whose relative abundances depend upon pH. Species 1 is exclusively present at pH ≤ 6, and remains in significant amoun...

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Hlavní autoři: Astashkin, Andrei V., Johnson-Winters, Kayunta, Klein, Eric L., Feng, Changjian, Wilson, Heather L., Rajagopalan, K. V., Raitsimring, Arnold M., Enemark, John H.
Médium: Artigo
Jazyk:Inglês
Vydáno: 2008
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2779766/
https://ncbi.nlm.nih.gov/pubmed/18529001
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja801406f
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