Accumulation of super(99)Mo-containing Iron-Molybdenum Cofactor Precursors of Nitrogenase on NifNE, NifH, and NifX of Azotobacter vinelandii
The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase was investigated using the purified in vitro FeMo-co synthesis system and super(99)Mo. The purified system involves the addition of all components that are known to be required for FeMo-co synthesis in their purified forms. He...
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| Published in | The Journal of biological chemistry Vol. 277; no. 42; pp. 40106 - 40111 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
18.10.2002
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| Online Access | Get full text |
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| Summary: | The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of nitrogenase was investigated using the purified in vitro FeMo-co synthesis system and super(99)Mo. The purified system involves the addition of all components that are known to be required for FeMo-co synthesis in their purified forms. Here, we report the accumulation of a super(99)Mo-containing FeMo-co precursor on NifNE. Apart from NifNE, NifH and NifX also accumulate super(99)Mo label. We present evidence that suggests NifH may serve as the entry point for molybdenum incorporation into the FeMo-co biosynthetic pathway. We also present evidence suggesting a role for NifX in specifying the organic acid moiety of FeMo-co. |
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| Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-1 |
| ISSN: | 0021-9258 |