تحميل...
Exploring by Pulsed EPR the Electronic Structure of Ubisemiquinone Bound at the Q(H) Site of Cytochrome bo(3) from Escherichia coli with in Vivo (13)C-Labeled Methyl and Methoxy Substituents
The cytochrome bo(3) ubiquinol oxidase from Escherichia coli resides in the bacterial cytoplasmic membrane and catalyzes the two-electron oxidation of ubiquinol-8 and four-electron reduction of O(2) to water. The one-electron reduced semiquinone forms transiently during the reaction, and the enzyme...
محفوظ في:
| المؤلفون الرئيسيون: | , , , , , , |
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| التنسيق: | Artigo |
| اللغة: | Inglês |
| منشور في: |
American Society for Biochemistry and Molecular Biology
2011
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3060462/ https://ncbi.nlm.nih.gov/pubmed/21247900 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M110.206821 |
| الوسوم: |
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