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PDBsum entry 1n2c

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Complex of nitrogenase proteins PDB id
1n2c

 

 

 

 

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Contents
Protein chains
478 a.a. *
522 a.a. *
274 a.a. *
Ligands
HCA ×2
CFM ×2
CLF ×2
ALF-ADP ×2
ALF ×2
SF4 ×2
ADP ×2
Metals
_CA ×2
_MG ×4
* Residue conservation analysis
PDB id:
1n2c
Name: Complex of nitrogenase proteins
Title: Nitrogenase complex from azotobacter vinelandii stabilized by adp- tetrafluoroaluminate
Structure: Nitrogenase molybdenum-iron protein. Chain: a, c. Fragment: chains a and c are the alpha chains, chains b and d are the beta chains. Synonym: nitrogenase component i, dinitrogenase. Nitrogenase molybdenum-iron protein. Chain: b, d. Fragment: chains a and c are the alpha chains, chains b and d are the beta chains.
Source: Azotobacter vinelandii. Organism_taxid: 354. Organism_taxid: 354
Biol. unit: Homo-Dimer (from PDB file)
Resolution:
3.00Å     R-factor:   0.208     R-free:   0.238
Authors: H.Schindelin,C.Kisker,D.C.Rees
Key ref: H.Schindelin et al. (1997). Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature, 387, 370-376. PubMed id: 9163420
Date:
02-May-97     Release date:   12-Nov-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P07328  (NIFD_AZOVI) -  Nitrogenase molybdenum-iron protein alpha chain from Azotobacter vinelandii
Seq:
Struc:
492 a.a.
478 a.a.
Protein chains
Pfam   ArchSchema ?
P07329  (NIFK_AZOVI) -  Nitrogenase molybdenum-iron protein beta chain from Azotobacter vinelandii
Seq:
Struc:
 
Seq:
Struc:
523 a.a.
522 a.a.
Protein chains
Pfam   ArchSchema ?
P00459  (NIFH1_AZOVI) -  Nitrogenase iron protein 1 from Azotobacter vinelandii
Seq:
Struc:
290 a.a.
274 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F, G, H: E.C.1.18.6.1  - nitrogenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Nitrogenase
      Reaction: N2 + 8 reduced [2Fe-2S]-[ferredoxin] + 16 ATP + 16 H2O = H2 + 8 oxidized [2Fe-2S]-[ferredoxin] + 2 NH4+ + 16 ADP + 16 phosphate + 6 H+
N2
+ 8 × reduced [2Fe-2S]-[ferredoxin]
+ 16 × ATP
+ 16 × H2O
= H2
Bound ligand (Het Group name = ADP)
corresponds exactly
+ 8 × oxidized [2Fe-2S]-[ferredoxin]
+ 2 × NH4(+)
+ 16 × ADP
+ 16 × phosphate
+ 6 × H(+)
      Cofactor: Iron-sulfur; Vanadium cation or Mo cation
Iron-sulfur
Vanadium cation
or Mo cation
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Nature 387:370-376 (1997)
PubMed id: 9163420  
 
 
Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction.
H.Schindelin, C.Kisker, J.L.Schlessman, J.B.Howard, D.C.Rees.
 
  ABSTRACT  
 
The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP x AIF4-, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The beta-phosphate and AIF4- groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21038112 K.Rupnik, Y.Hu, A.W.Fay, M.W.Ribbe, and B.J.Hales (2011).
Variable-temperature, variable-field magnetic circular dichroism spectroscopic study of NifEN-bound precursor and "FeMoco".
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21248230 M.A.Saito, E.M.Bertrand, S.Dutkiewicz, V.V.Bulygin, D.M.Moran, F.M.Monteiro, M.J.Follows, F.W.Valois, and J.B.Waterbury (2011).
Iron conservation by reduction of metalloenzyme inventories in the marine diazotroph Crocosphaera watsonii.
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21276251 N.Pawlowski, A.Khaminets, J.P.Hunn, N.Papic, A.Schmidt, R.C.Uthaiah, R.Lange, G.Vopper, S.Martens, E.Wolf, and J.C.Howard (2011).
The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii.
  BMC Biol, 9, 7.  
21231967 W.Wu, K.T.Park, T.Holyoak, and J.Lutkenhaus (2011).
Determination of the structure of the MinD-ATP complex reveals the orientation of MinD on the membrane and the relative location of the binding sites for MinE and MinC.
  Mol Microbiol, 79, 1515-1528.
PDB code: 3q9l
20221547 A.W.Fay, M.A.Blank, J.M.Yoshizawa, C.C.Lee, J.A.Wiig, Y.Hu, K.O.Hodgson, B.Hedman, and M.W.Ribbe (2010).
Formation of a homocitrate-free iron-molybdenum cluster on NifEN: implications for the role of homocitrate in nitrogenase assembly.
  Dalton Trans, 39, 3124-3130.  
20146278 J.Kim, A.J.Pierik, and W.Buckel (2010).
A complex of 2-hydroxyisocaproyl-coenzyme A dehydratase and its activator from Clostridium difficile stabilized by aluminium tetrafluoride-adenosine diphosphate.
  Chemphyschem, 11, 1307-1312.  
20075073 M.J.Bröcker, D.Wätzlich, M.Saggu, F.Lendzian, J.Moser, and D.Jahn (2010).
Biosynthesis of (bacterio)chlorophylls: ATP-dependent transient subunit interaction and electron transfer of dark operative protochlorophyllide oxidoreductase.
  J Biol Chem, 285, 8268-8277.  
20023013 P.F.Teixeira, H.Wang, and S.Nordlund (2010).
Nitrogenase switch-off and regulation of ammonium assimilation in response to light deprivation in Rhodospirillum rubrum are influenced by the nitrogen source used during growth.
  J Bacteriol, 192, 1463-1466.  
20221527 Y.Hu, A.W.Fay, C.C.Lee, J.A.Wiig, and M.W.Ribbe (2010).
Dual functions of NifEN: insights into the evolution and mechanism of nitrogenase.
  Dalton Trans, 39, 2964-2971.  
20030377 Y.Hu, and M.W.Ribbe (2010).
Decoding the nitrogenase mechanism: the homologue approach.
  Acc Chem Res, 43, 475-484.  
19675567 A.Mateja, A.Szlachcic, M.E.Downing, M.Dobosz, M.Mariappan, R.S.Hegde, and R.J.Keenan (2009).
The structural basis of tail-anchored membrane protein recognition by Get3.
  Nature, 461, 361-366.
PDB codes: 2woj 2woo
19706470 C.J.Suloway, J.W.Chartron, M.Zaslaver, and W.M.Clemons (2009).
Model for eukaryotic tail-anchored protein binding based on the structure of Get3.
  Proc Natl Acad Sci U S A, 106, 14849-14854.
PDB codes: 3ibg 3idq
19525115 D.C.Lee, and Z.Jia (2009).
Emerging structural insights into bacterial tyrosine kinases.
  Trends Biochem Sci, 34, 351-357.  
19234479 D.C.Rees, E.Johnson, and O.Lewinson (2009).
ABC transporters: the power to change.
  Nat Rev Mol Cell Biol, 10, 218-227.  
19336405 D.Wätzlich, M.J.Bröcker, F.Uliczka, M.Ribbe, S.Virus, D.Jahn, and J.Moser (2009).
Chimeric nitrogenase-like enzymes of (bacterio)chlorophyll biosynthesis.
  J Biol Chem, 284, 15530-15540.  
19675644 G.Schwarz, R.R.Mendel, and M.W.Ribbe (2009).
Molybdenum cofactors, enzymes and pathways.
  Nature, 460, 839-847.  
19181830 H.Dang, X.Luan, J.Zhao, and J.Li (2009).
Diverse and novel nifH and nifH-like gene sequences in the deep-sea methane seep sediments of the Okhotsk Sea.
  Appl Environ Microbiol, 75, 2238-2245.  
19783748 J.Miyazaki, R.Higa, T.Toki, J.Ashi, U.Tsunogai, T.Nunoura, H.Imachi, and K.Takai (2009).
Molecular characterization of potential nitrogen fixation by anaerobic methane-oxidizing archaea in the methane seep sediments at the number 8 Kumano Knoll in the Kumano Basin, offshore of Japan.
  Appl Environ Microbiol, 75, 7153-7162.  
19489731 L.C.Seefeldt, B.M.Hoffman, and D.R.Dean (2009).
Mechanism of Mo-dependent nitrogenase.
  Annu Rev Biochem, 78, 701-722.  
19424291 R.Gasper, S.Meyer, K.Gotthardt, M.Sirajuddin, and A.Wittinghofer (2009).
It takes two to tango: regulation of G proteins by dimerization.
  Nat Rev Mol Cell Biol, 10, 423-429.  
19805110 Y.Hu, J.M.Yoshizawa, A.W.Fay, C.C.Lee, J.A.Wiig, and M.W.Ribbe (2009).
Catalytic activities of NifEN: implications for nitrogenase evolution and mechanism.
  Proc Natl Acad Sci U S A, 106, 16962-16966.  
18386081 J.Petersen, C.J.Mitchell, K.Fisher, and D.J.Lowe (2008).
Structural basis for VO(2+)-inhibition of nitrogenase activity: (B) pH-sensitive inner-sphere rearrangements in the 1H-environment of the metal coordination site of the nitrogenase Fe-protein identified by ENDOR spectroscopy.
  J Biol Inorg Chem, 13, 637-650.  
18351402 J.Petersen, K.Fisher, and D.J.Lowe (2008).
Structural basis for VO2+ inhibition of nitrogenase activity (A): 31P and 23Na interactions with the metal at the nucleotide binding site of the nitrogenase Fe protein identified by ENDOR spectroscopy.
  J Biol Inorg Chem, 13, 623-635.  
18485075 J.W.Hickman, and C.S.Harwood (2008).
Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor.
  Mol Microbiol, 69, 376-389.  
18274792 M.Hans, W.Buckel, and E.Bill (2008).
Spectroscopic evidence for an all-ferrous [4Fe-4S]0 cluster in the superreduced activator of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans.
  J Biol Inorg Chem, 13, 563-574.  
18713389 Q.Cheng (2008).
Perspectives in biological nitrogen fixation research.
  J Integr Plant Biol, 50, 786-798.  
17151076 C.G.Noble, B.Beuth, and I.A.Taylor (2007).
Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor.
  Nucleic Acids Res, 35, 87-99.
PDB code: 2npi
17614310 I.Dance (2007).
Elucidating the coordination chemistry and mechanism of biological nitrogen fixation.
  Chem Asian J, 2, 936-946.  
17328675 J.Lutkenhaus (2007).
Assembly dynamics of the bacterial MinCDE system and spatial regulation of the Z ring.
  Annu Rev Biochem, 76, 539-562.  
17991025 T.Shi, Y.Sun, and P.G.Falkowski (2007).
Effects of iron limitation on the expression of metabolic genes in the marine cyanobacterium Trichodesmium erythraeum IMS101.
  Environ Microbiol, 9, 2945-2956.  
16688314 B.M.Barney, H.I.Lee, P.C.Dos Santos, B.M.Hoffman, D.R.Dean, and L.C.Seefeldt (2006).
Breaking the N2 triple bond: insights into the nitrogenase mechanism.
  Dalton Trans, (), 2277-2284.  
17088547 J.B.Howard, and D.C.Rees (2006).
How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation.
  Proc Natl Acad Sci U S A, 103, 17088-17093.  
16510305 J.W.Peters, and R.K.Szilagyi (2006).
Exploring new frontiers of nitrogenase structure and mechanism.
  Curr Opin Chem Biol, 10, 101-108.  
17009470 K.Fisher, D.J.Lowe, and J.Petersen (2006).
Vanadium (V) is reduced by the 'as isolated' nitrogenase Fe-protein at neutral pH.
  Chem Commun (Camb), (), 2807-2809.  
16885471 N.Gavini, S.Tungtur, and L.Pulakat (2006).
Peptidyl-prolyl cis/trans isomerase-independent functional NifH mutant of Azotobacter vinelandii.
  J Bacteriol, 188, 6020-6025.  
16677298 P.S.Lee, and A.D.Grossman (2006).
The chromosome partitioning proteins Soj (ParA) and Spo0J (ParB) contribute to accurate chromosome partitioning, separation of replicated sister origins, and regulation of replication initiation in Bacillus subtilis.
  Mol Microbiol, 60, 853-869.  
16807243 R.Gasper, A.Scrima, and A.Wittinghofer (2006).
Structural insights into HypB, a GTP-binding protein that regulates metal binding.
  J Biol Chem, 281, 27492-27502.
PDB codes: 2hf8 2hf9
16983380 S.J.Lippard (2006).
The inorganic side of chemical biology.
  Nat Chem Biol, 2, 504-507.  
16315272 S.Sen, and J.W.Peters (2006).
The thermal adaptation of the nitrogenase Fe protein from thermophilic Methanobacter thermoautotrophicus.
  Proteins, 62, 450-460.  
16704345 W.Buckel, and B.T.Golding (2006).
Radical enzymes in anaerobes.
  Annu Rev Microbiol, 60, 27-49.  
16123301 F.A.Tezcan, J.T.Kaiser, D.Mustafi, M.Y.Walton, J.B.Howard, and D.C.Rees (2005).
Nitrogenase complexes: multiple docking sites for a nucleotide switch protein.
  Science, 309, 1377-1380.
PDB codes: 2afh 2afi 2afk 4wzb
15805531 H.Zhou, and J.Lutkenhaus (2005).
MinC mutants deficient in MinD- and DicB-mediated cell division inhibition due to loss of interaction with MinD, DicB, or a septal component.
  J Bacteriol, 187, 2846-2857.  
15629934 H.Zhou, R.Schulze, S.Cox, C.Saez, Z.Hu, and J.Lutkenhaus (2005).
Analysis of MinD mutations reveals residues required for MinE stimulation of the MinD ATPase and residues required for MinC interaction.
  J Bacteriol, 187, 629-638.  
15867150 L.J.Vitt, and E.R.Pianka (2005).
Deep history impacts present-day ecology and biodiversity.
  Proc Natl Acad Sci U S A, 102, 7877-7881.  
15897178 T.A.Leonard, J.Møller-Jensen, and J.Löwe (2005).
Towards understanding the molecular basis of bacterial DNA segregation.
  Philos Trans R Soc Lond B Biol Sci, 360, 523-535.  
15635448 T.A.Leonard, P.J.Butler, and J.Löwe (2005).
Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch.
  EMBO J, 24, 270-282.
PDB codes: 1wcv 2bej 2bek
16218867 W.Buckel, B.M.Martins, A.Messerschmidt, and B.T.Golding (2005).
Radical-mediated dehydration reactions in anaerobic bacteria.
  Biol Chem, 386, 951-959.  
15887041 Z.Maskos, K.Fisher, M.Sørlie, W.E.Newton, and B.J.Hales (2005).
Variant MoFe proteins of Azotobacter vinelandii: effects of carbon monoxide on electron paramagnetic resonance spectra generated during enzyme turnover.
  J Biol Inorg Chem, 10, 394-406.  
  15374661 J.Kim, M.Hetzel, C.D.Boiangiu, and W.Buckel (2004).
Dehydration of (R)-2-hydroxyacyl-CoA to enoyl-CoA in the fermentation of alpha-amino acids by anaerobic bacteria.
  FEMS Microbiol Rev, 28, 455-468.  
15489428 J.Szeto, S.Acharya, N.F.Eng, and J.A.Dillon (2004).
The N terminus of MinD contains determinants which affect its dynamic localization and enzymatic activity.
  J Bacteriol, 186, 7175-7185.  
15557555 L.J.Vitt (2004).
Shifting paradigms: Herbivory and body size in lizards.
  Proc Natl Acad Sci U S A, 101, 16713-16714.  
15458408 L.Ma, G.F.King, and L.Rothfield (2004).
Positioning of the MinE binding site on the MinD surface suggests a plausible mechanism for activation of the Escherichia coli MinD ATPase during division site selection.
  Mol Microbiol, 54, 99.  
15558053 M.A.Oliva, S.C.Cordell, and J.Löwe (2004).
Structural insights into FtsZ protofilament formation.
  Nat Struct Mol Biol, 11, 1243-1250.
PDB codes: 1w58 1w59 1w5a 1w5b 1w5e 1w5f
14724630 P.F.Egea, S.O.Shan, J.Napetschnig, D.F.Savage, P.Walter, and R.M.Stroud (2004).
Substrate twinning activates the signal recognition particle and its receptor.
  Nature, 427, 215-221.
PDB code: 1rj9
15263897 R.Dixon, and D.Kahn (2004).
Genetic regulation of biological nitrogen fixation.
  Nat Rev Microbiol, 2, 621-631.  
15549494 S.B.Jang, M.S.Jeong, L.C.Seefeldt, and J.W.Peters (2004).
Structural and biochemical implications of single amino acid substitutions in the nucleotide-dependent switch regions of the nitrogenase Fe protein from Azotobacter vinelandii.
  J Biol Inorg Chem, 9, 1028-1033.
PDB codes: 1xd8 1xd9 1xdb
12675792 J.Lutkenhaus, and M.Sundaramoorthy (2003).
MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation.
  Mol Microbiol, 48, 295-303.  
14526036 Y.K.Wang, S.Park, B.T.Nixon, and T.R.Hoover (2003).
Nucleotide-dependent conformational changes in the sigma54-dependent activator DctD.
  J Bacteriol, 185, 6215-6219.  
12486056 Z.Hu, C.Saez, and J.Lutkenhaus (2003).
Recruitment of MinC, an inhibitor of Z-ring formation, to the membrane in Escherichia coli: role of MinD and MinE.
  J Bacteriol, 185, 196-203.  
12519187 Z.Hu, and J.Lutkenhaus (2003).
A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum.
  Mol Microbiol, 47, 345-355.  
11844750 A.L.Davidson (2002).
Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters.
  J Bacteriol, 184, 1225-1233.  
12270840 A.Ureta, and S.Nordlund (2002).
Evidence for conformational protection of nitrogenase against oxygen in Gluconacetobacter diazotrophicus by a putative FeSII protein.
  J Bacteriol, 184, 5805-5809.  
12045096 D.C.Rees (2002).
Great metalloclusters in enzymology.
  Annu Rev Biochem, 71, 221-246.  
12403627 J.Petersen, K.Fisher, C.J.Mitchell, and D.J.Lowe (2002).
Multiple inequivalent metal-nucleotide coordination environments in the presence of the VO2+-inhibited nitrogenase iron protein: pH-dependent structural rearrangements at the nucleotide binding site.
  Biochemistry, 41, 13253-13263.  
12004122 K.P.Locher, A.T.Lee, and D.C.Rees (2002).
The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism.
  Science, 296, 1091-1098.
PDB code: 1l7v
12039013 L.Noodleman, T.Lovell, T.Liu, F.Himo, and R.A.Torres (2002).
Insights into properties and energetics of iron-sulfur proteins from simple clusters to nitrogenase.
  Curr Opin Chem Biol, 6, 259-273.  
11980491 M.Hans, E.Bill, I.Cirpus, A.J.Pierik, M.Hetzel, D.Alber, and W.Buckel (2002).
Adenosine triphosphate-induced electron transfer in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans.
  Biochemistry, 41, 5873-5882.  
11978793 M.W.Ribbe, Y.Hu, M.Guo, B.Schmid, and B.K.Burgess (2002).
The FeMoco-deficient MoFe protein produced by a nifH deletion strain of Azotobacter vinelandii shows unusual P-cluster features.
  J Biol Chem, 277, 23469-23476.  
11812780 T.Brinkmann, O.Daumke, U.Herbrand, D.Kühlmann, P.Stege, M.R.Ahmadian, and A.Wittinghofer (2002).
Rap-specific GTPase activating protein follows an alternative mechanism.
  J Biol Chem, 277, 12525-12531.  
12475211 V.L.Davidson (2002).
Chemically gated electron transfer. A means of accelerating and regulating rates of biological electron transfer.
  Biochemistry, 41, 14633-14636.  
11532954 E.Fung, J.Y.Bouet, and B.E.Funnell (2001).
Probing the ATP-binding site of P1 ParA: partition and repression have different requirements for ATP binding and hydrolysis.
  EMBO J, 20, 4901-4911.  
11170380 H.Chiu, J.W.Peters, W.N.Lanzilotta, M.J.Ryle, L.C.Seefeldt, J.B.Howard, and D.C.Rees (2001).
MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127 Delta-Fe-protein and the MoFe-protein.
  Biochemistry, 40, 641-650.
PDB codes: 1g20 1g21
11296216 I.Hayashi, T.Oyama, and K.Morikawa (2001).
Structural and functional studies of MinD ATPase: implications for the molecular recognition of the bacterial cell division apparatus.
  EMBO J, 20, 1819-1828.
PDB codes: 1g3q 1g3r
11171984 J.Chen, S.Sharma, F.A.Quiocho, and A.L.Davidson (2001).
Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport.
  Proc Natl Acad Sci U S A, 98, 1525-1530.  
11337399 J.Christiansen, D.R.Dean, and L.C.Seefeldt (2001).
MECHANISTIC FEATURES OF THE MO-CONTAINING NITROGENASE.
  Annu Rev Plant Physiol Plant Mol Biol, 52, 269-295.  
11258953 K.Fisher, W.E.Newton, and D.J.Lowe (2001).
Electron paramagnetic resonance analysis of different Azotobacter vinelandii nitrogenase MoFe-protein conformations generated during enzyme turnover: evidence for S = 3/2 spin states from reduced MoFe-protein intermediates.
  Biochemistry, 40, 3333-3339.  
11500892 M.Goez, and V.Zubarev (2001).
Double Photoionization of Dimethylaminobenzonitrile in Solution: A Three-Quantum Process with Intervening Chemical Step This work was supported by the Volkswagenstiftung.
  Angew Chem Int Ed Engl, 40, 2867-2869.  
11170381 P.Strop, P.M.Takahara, H.Chiu, H.C.Angove, B.K.Burgess, and D.C.Rees (2001).
Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase iron protein from Azotobacter vinelandii.
  Biochemistry, 40, 651-656.
PDB codes: 1g1m 1g5p
11168422 R.W.Miller, R.R.Eady, S.A.Fairhurst, C.A.Gormal, and B.E.Smith (2001).
Transition state complexes of the Klebsiella pneumoniae nitrogenase proteins. Spectroscopic properties of aluminium fluoride-stabilized and beryllium fluoride-stabilized MgADP complexes reveal conformational differences of the Fe protein.
  Eur J Biochem, 268, 809-818.  
11277916 S.Siemann, K.Schneider, K.Behrens, A.Knöchel, W.Klipp, and A.Müller (2001).
FeMo cofactor biosynthesis in a nifE- mutant of Rhodobacter capsulatus.
  Eur J Biochem, 268, 1940-1952.  
  11557766 T.Murata, Y.Kakinuma, and I.Yamato (2001).
ATP-dependent affinity change of Na+-binding sites of V-ATPase.
  J Biol Chem, 276, 48337-48340.  
11006545 D.C.Rees, and J.B.Howard (2000).
Nitrogenase: standing at the crossroads.
  Curr Opin Chem Biol, 4, 559-566.  
10838059 E.Muneyuki, H.Noji, T.Amano, T.Masaike, and M.Yoshida (2000).
F(0)F(1)-ATP synthase: general structural features of 'ATP-engine' and a problem on free energy transduction.
  Biochim Biophys Acta, 1458, 467-481.  
10801496 G.Montoya, K.Kaat, R.Moll, G.Schäfer, and I.Sinning (2000).
The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP-SRP receptor complex.
  Structure, 8, 515-525.
PDB codes: 1j8m 1j8y
11087938 J.L.Johnson, A.C.Nyborg, P.E.Wilson, A.M.Tolley, F.R.Nordmeyer, and G.D.Watt (2000).
Analysis of steady state Fe and MoFe protein interactions during nitrogenase catalysis.
  Biochim Biophys Acta, 1543, 24-35.  
10852721 J.M.Chan, W.Wu, D.R.Dean, and L.C.Seefeldt (2000).
Construction and characterization of a heterodimeric iron protein: defining roles for adenosine triphosphate in nitrogenase catalysis.
  Biochemistry, 39, 7221-7228.  
10713991 K.A.Denessiouk, and M.S.Johnson (2000).
When fold is not important: a common structural framework for adenine and AMP binding in 12 unrelated protein families.
  Proteins, 38, 310-326.  
10873854 K.Braig, R.I.Menz, M.G.Montgomery, A.G.Leslie, and J.E.Walker (2000).
Structure of bovine mitochondrial F(1)-ATPase inhibited by Mg(2+) ADP and aluminium fluoride.
  Structure, 8, 567-573.
PDB codes: 1e1q 1e1r
10978172 K.Fisher, M.J.Dilworth, C.H.Kim, and W.E.Newton (2000).
Azotobacter vinelandii nitrogenases with substitutions in the FeMo-cofactor environment of the MoFe protein: effects of acetylene or ethylene on interactions with H+, HCN, and CN-.
  Biochemistry, 39, 10855-10865.  
11112544 K.Fisher, M.J.Dilworth, and W.E.Newton (2000).
Differential effects on N(2) binding and reduction, HD formation, and azide reduction with alpha-195(His)- and alpha-191(Gln)-substituted MoFe proteins of Azotobacter vinelandii nitrogenase.
  Biochemistry, 39, 15570-15577.  
  10739254 L.Zou, M.C.Baguinon, X.Guo, S.Y.Guo, Y.Yu, and L.C.Davis (2000).
Interaction with magnesium and ADP stabilizes both components of nitrogenase from Klebsiella pneumoniae against urea denaturation.
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11001306 L.Zou, S.Y.Guo, and L.C.Davis (2000).
Using electrophoresis to observe the interaction of nitrogenase with ions.
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The iron-sulfur clusters in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Biochemical and spectroscopic investigations.
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Hydrolysis of nucleoside triphosphates other than ATP by nitrogenase.
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10837496 M.W.Ribbe, E.H.Bursey, and B.K.Burgess (2000).
Identification of an Fe protein residue (Glu146) of Azotobacter vinelandii nitrogenase that is specifically involved in FeMo cofactor insertion.
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10956051 R.Camba, and F.A.Armstrong (2000).
Investigations of the oxidative disassembly of Fe-S clusters in Clostridium pasteurianum 8Fe ferredoxin using pulsed-protein-film voltammetry.
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11101289 S.B.Jang, L.C.Seefeldt, and J.W.Peters (2000).
Insights into nucleotide signal transduction in nitrogenase: structure of an iron protein with MgADP bound.
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PDB code: 1fp6
10924155 S.Nadanaciva, J.Weber, and A.E.Senior (2000).
New probes of the F1-ATPase catalytic transition state reveal that two of the three catalytic sites can assume a transition state conformation simultaneously.
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10985789 T.A.Clarke, S.Maritano, and R.R.Eady (2000).
Formation of a tight 1:1 complex of Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein: evidence for long-range interactions between the Fe protein binding sites during catalytic hydrogen evolution.
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10970874 T.Zhou, S.Radaev, B.P.Rosen, and D.L.Gatti (2000).
Structure of the ArsA ATPase: the catalytic subunit of a heavy metal resistance pump.
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PDB code: 1f48
  10419963 I.Rombel, P.Peters-Wendisch, A.Mesecar, T.Thorgeirsson, Y.K.Shin, and S.Kustu (1999).
MgATP binding and hydrolysis determinants of NtrC, a bacterial enhancer-binding protein.
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10336305 J.G.Grossman, S.S.Hasnain, F.K.Yousafzai, B.E.Smith, R.R.Eady, H.Schindelin, C.Kisker, J.G.Howard, H.Tsuruta, J.Muller, and D.C.Rees (1999).
Comparing crystallographic and solution structures of nitrogenase complexes.
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10231529 J.M.Chan, J.Christiansen, D.R.Dean, and L.C.Seefeldt (1999).
Spectroscopic evidence for changes in the redox state of the nitrogenase P-cluster during turnover.
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Evidence that MgATP accelerates primary electron transfer in a Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein nitrogenase tight complex.
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Inhibition of iron-molybdenum cofactor biosynthesis by L127Delta NifH and evidence for a complex formation between L127Delta NifH and NifNE.
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The crystal structure of rna1p: a new fold for a GTPase-activating protein.
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PDB code: 1yrg
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Genetic analysis of nif regulatory genes by utilizing the yeast two-hybrid system detected formation of a NifL-NifA complex that is implicated in regulated expression of nif genes.
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Binding of the transition state analog MgADP-fluoroaluminate to F1-ATPase.
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Characterization of a variant iron protein of nitrogenase that is impaired in its ability to adopt the MgATP-induced conformational change.
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The role of methionine 156 in cross-subunit nucleotide interactions in the iron protein of nitrogenase.
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An all-ferrous state of the Fe protein of nitrogenase. Interaction with nucleotides and electron transfer to the MoFe protein.
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14N electron spin-echo envelope modulation of the S = 3/2 spin system of the Azotobacter vinelandii nitrogenase iron-molybdenum cofactor.
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Iron-sulfur proteins: new roles for old clusters.
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Nitrogen cycle enzymology.
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Active sites of transition-metal enzymes with a focus on nickel.
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Evidence for coupled electron and proton transfer in the [8Fe-7S] cluster of nitrogenase.
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9382787 A.Wittinghofer (1997).
Signaling mechanistics: aluminum fluoride for molecule of the year.
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9325305 J.A.Kelley, and K.L.Knight (1997).
Allosteric regulation of RecA protein function is mediated by Gln194.
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Novel mechanism for carbamoyl-phosphate synthetase: a nucleotide switch for functionally equivalent domains.
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9335529 V.L.Davidson, L.H.Jones, M.E.Graichen, F.S.Mathews, and J.P.Hosler (1997).
Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis.
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Changes in the midpoint potentials of the nitrogenase metal centers as a result of iron protein-molybdenum-iron protein complex formation.
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The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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