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Characterization of chloride-depleted human sulfite oxidase by EPR spectroscopy: experimental evidence for the role of anions in product release

The Mo(V) state of the molybdoenzyme sulfite oxidase (SO) is paramagnetic and can be studied by electron paramagnetic resonance (EPR) spectroscopy. Vertebrate SO at pH < 7 and pH > 9 exhibits characteristic EPR spectra that correspond to two structurally different forms of the Mo(V) active cen...

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書誌詳細
主要な著者: Rajapakshe, Asha, Johnson-Winters, Kayunta, Nordstrom, Anna R., Meyers, Kimberly T., Emesh, Safia, Astashkin, Andrei V., Enemark, John H.
フォーマット: Artigo
言語:Inglês
出版事項: 2010
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC2890295/
https://ncbi.nlm.nih.gov/pubmed/20491442
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi902172n
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