Pulsed EPR Studies of a Bacterial Sulfite-Oxidizing Enzyme with pH-Invariant Hyperfine Interactions from Exchangeable Protons

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• 作者：Arnold M. Raitsimring ; Ulrike Kappler ; Changjian Feng ; Andrei V. Astashkin ; and John H. Enemark
• 刊名：Inorganic Chemistry
• 出版年：2005
• 出版时间：October 17, 2005
• 年：2005
• 卷：44
• 期：21
• 页码：7283 - 7285
• 全文大小：43K
• 年卷期：v.44,no.21(October 17, 2005)
• ISSN：1520-510X

文摘

Variable-frequency pulsed electron paramagnetic resonance studiesof the molybdenum(V) center of sulfite dehydrogenase (SDH)clearly show couplings from nearby exchangeable protons thatare assigned to a Mo^VOH_n group. The hyperfine parameters forthese exchangeable protons of SDH are the same at both lowand high pH and similar to those for the high-pH forms of sulfiteoxidases (SOs) from eukaryotes. The SDH proton parameters aredistinctly different from the low-pH forms of chicken and humanSO.