The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
The structure of vanadium nitrogenase reveals an unusual bridging ligand
Open accessAbstract
Nitrogenases catalyze the reduction of N2 gas to ammonium at a complex heterometallic cofactor. Most commonly this is the FeMo cofactor (FeMoco), a [Mo:7Fe:9S:C] cluster whose exact reactivity and substrate binding mode remain unknown. Alternative nitrogenases replace molybdenum with either vanadium or iron and differ in reactivity, prominently in the ability of vanadium nitrogenase to reduce CO to hydrocarbons. Here we report the 1.35 Å structure of vanadium nitrogenase from Azotobacter vinelandii. The 240 kDa protein contains an additional α-helical subunit not present in molybdenum nitrogenase. The FeV cofactor (FeVco) is a [V:7Fe:8S:C] cluster with a homocitrate ligand to vanadium. Unexpectedly, it lacks one sulfide ion compared to FeMoco that is replaced by a bridging ligand, likely a μ-1,3-carbonate. The anion fits into a pocket within the protein that is obstructed in molybdenum nitrogenase, and its different chemical character helps to rationalize the altered chemical properties of this unique N2- and CO-fixing enzyme.
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Nitrogenase Bioelectrochemistry for Synthesis Applications
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Structural insights into the iron nitrogenase complex
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Metadata
- Authors
- Sippel, D., & Einsle, O.
- Venue
- Nature Chemical Biology
- Published
- 2017-07-10
- Volume
- 13
- Issue
- 9
- Pages
- 956-960
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- OpenAlex
- W2734386232
- Cited by
- 282
- References
- 49
- FWCI
- 8.61
- Type
- journal article
- Language
- en
- Open access
- green
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