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Descripción
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| NifB utilizes two equivalents of S-adenosyl methionine (SAM) to insert a carbide atom and fuse two substrate [Fe?S] clusters forming the NifB cofactor (NifB-co), which is then passed to NifEN for further modification to form the iron?molybdenum cofactor (FeMo-co) of nitrogenase. Here, we demonstrate that NifB from the methanogen Methanocaldococcus infernus is a radical SAM enzyme able to reductively cleave SAM to 5?-deoxyadenosine radical and is competent in FeMo-co maturation. Using electron paramagnetic resonance spectroscopy we have characterized three [4Fe?4S] clusters, one SAM binding cluster, and two auxiliary clusters probably acting as substrates for NifB-co formation. Nitrogen coordination to one or more of the auxiliary clusters in NifB was observed, and its mechanistic implications for NifB-co dissociation from the maturase are discussed. | |
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Internacional
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Si |
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JCR del ISI
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Si |
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Título de la revista
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Journal of the American Chemical Society |
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ISSN
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0002-7863 |
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Factor de impacto JCR
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11,444 |
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Información de impacto
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Datos JCR del año 2013 |
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Volumen
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138 |
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DOI
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10.1021/jacs.6b03329 |
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Número de revista
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24 |
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Desde la página
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7468 |
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Hasta la página
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7471 |
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Mes
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JUNIO |
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Ranking
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