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Descripción
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| Nitrogenase carries at its active site a unique iron?molybdenum cofactor (FeMo-co) that consists of an inorganic 7 Fe, 1 Mo, 1 C, 9 S core coordinated to the organic acid homocitrate. Biosynthesis of FeMo-co occurs outside nitrogenase through a complex pathway involving proteins acting as molecular scaffolds, as metallocluster carriers, or enzymes to provide substrates in appropriate chemical forms. Insertion of completed FeMo-co into a P-cluster containing but FeMo-co-deficient NifDK polypeptide results in nitrogenase reconstitution. Investigation of FeMo-co biosynthesis has uncovered new radical chemistry reactions and new roles for iron?sulfur clusters in biology. | |
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Internacional
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Si |
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DOI
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Edición del Libro
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Editorial del Libro
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John Wiley & Sons, Inc |
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ISBN
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9781119053095 |
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Serie
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Título del Libro
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Biological Nitrogen Fixation |
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Desde página
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75 |
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Hasta página
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86 |