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TitleArchitecture of the RNF1 complex that drives biological nitrogen fixation.
Journal, issue, pagesNat Chem Biol, Year 2024
Publish dateJun 18, 2024
AuthorsLin Zhang / Oliver Einsle /
PubMed AbstractBiological nitrogen fixation requires substantial metabolic energy in form of ATP as well as low-potential electrons that must derive from central metabolism. During aerobic growth, the free-living ...Biological nitrogen fixation requires substantial metabolic energy in form of ATP as well as low-potential electrons that must derive from central metabolism. During aerobic growth, the free-living soil diazotroph Azotobacter vinelandii transfers electrons from the key metabolite NADH to the low-potential ferredoxin FdxA that serves as a direct electron donor to the dinitrogenase reductases. This process is mediated by the RNF complex that exploits the proton motive force over the cytoplasmic membrane to lower the midpoint potential of the transferred electron. Here we report the cryogenic electron microscopy structure of the nitrogenase-associated RNF complex of A. vinelandii, a seven-subunit membrane protein assembly that contains four flavin cofactors and six iron-sulfur centers. Its function requires the strict coupling of electron and proton transfer but also involves major conformational changes within the assembly that can be traced with a combination of electron microscopy and modeling.
External linksNat Chem Biol / PubMed:38890433
MethodsEM (single particle)
Resolution3.11 - 3.41 Å
Structure data

15452

8ahx

EMDB-15452, PDB-8ahx:
Cryo-EM structure of the nitrogen-fixation associated NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii
Method: EM (single particle) / Resolution: 3.11 Å

19028

8rb8

EMDB-19028, PDB-8rb8:
Cryo-EM structure of the NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii, purified with 2-ME/TCEP, NADH added
Method: EM (single particle) / Resolution: 3.41 Å

19029

8rb9

EMDB-19029, PDB-8rb9:
Cryo-EM structure of the NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii, NADH added
Method: EM (single particle) / Resolution: 3.19 Å

19032

8rbm

EMDB-19032, PDB-8rbm:
Cryo-EM structure of the NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii, ferricyanide oxidized
Method: EM (single particle) / Resolution: 3.24 Å

19034

8rbq

EMDB-19034, PDB-8rbq:
Cryo-EM structure of the NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii, dithionite reduced
Method: EM (single particle) / Resolution: 3.32 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-RBF:
RIBOFLAVIN

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

Source
  • azotobacter vinelandii dj (bacteria)
KeywordsMEMBRANE PROTEIN / metalloprotein / flavoprotein / electron transfer and Na+/H+ translocation / NADH:ferredoxin oxidoreductase

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