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TitleStructural insights into the iron nitrogenase complex.
Journal, issue, pagesNat Struct Mol Biol, Vol. 31, Issue 1, Page 150-158, Year 2024
Publish dateDec 7, 2023
AuthorsFrederik V Schmidt / Luca Schulz / Jan Zarzycki / Simone Prinz / Niels N Oehlmann / Tobias J Erb / Johannes G Rebelein /
PubMed AbstractNitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO) and carbon monoxide ...Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO) and carbon monoxide to hydrocarbons, offering a pathway to recycle carbon waste into hydrocarbon products. Among the three nitrogenase isozymes, the iron nitrogenase has the highest wild-type activity for the reduction of CO, but the molecular architecture facilitating these activities has remained unknown. Here, we report a 2.35-Å cryogenic electron microscopy structure of the ADP·AlF-stabilized iron nitrogenase complex from Rhodobacter capsulatus, revealing an [FeSC-(R)-homocitrate] cluster in the active site. The enzyme complex suggests that the iron nitrogenase G subunit is involved in cluster stabilization and substrate channeling and confers specificity between nitrogenase reductase and catalytic component proteins. Moreover, the structure highlights a different interface between the two catalytic halves of the iron and the molybdenum nitrogenase, potentially influencing the intrasubunit 'communication' and thus the nitrogenase mechanism.
External linksNat Struct Mol Biol / PubMed:38062208 / PubMed Central
MethodsEM (single particle)
Resolution2.35 - 2.49 Å
Structure data

16890

8oie

EMDB-16890, PDB-8oie:
Iron Nitrogenase Complex from Rhodobacter capsulatus
Method: EM (single particle) / Resolution: 2.35 Å

17583

8pbb

EMDB-17583, PDB-8pbb:
CHAPSO treated partial catalytic component (comprising only AnfD & AnfK, lacking AnfG and FeFeco) of iron nitrogenase from Rhodobacter capsulatus
Method: EM (single particle) / Resolution: 2.49 Å

Chemicals

ChemComp-S5Q:
FeFe cofactor

ChemComp-HCA:
3-HYDROXY-3-CARBOXY-ADIPIC ACID

ChemComp-CLF:
FE(8)-S(7) CLUSTER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-MG:
Unknown entry

ChemComp-AF3:
ALUMINUM FLUORIDE / Aluminium fluoride

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-HOH:
WATER / Water

Source
  • rhodobacter capsulatus sb 1003 (bacteria)
KeywordsOXIDOREDUCTASE / nitrogen fixation / Fe nitrogenase

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