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Evidence for Redox Cooperativity between c-Type Hemes of MauG which is Likely Coupled to Oxygen Activation during Tryptophan Tryptophylquinone Biosynthesis

MauG is a novel 42 kDa di-heme protein which is required for the biosynthesis of tryptophan tryptophylquinone, the prosthetic group of methylamine dehydrogenase. The visible absorption and resonance Raman spectroscopic properties of each of the two c-type hemes, and the overall redox properties of M...

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Библиографические подробности
Главные авторы: Li, Xianghui, Feng, Manliang, Wang, Yongting, Tachikawa, Hiroyasu, Davidson, Victor L.
Формат: Artigo
Язык:Inglês
Опубликовано: 2006
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Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2565495/
https://ncbi.nlm.nih.gov/pubmed/16411758
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi052000n
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