IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli. Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli. The Journal of biological chemistry 2007 imex curation Jepson BJ., Mohan S., Clarke TA., Gates AJ., Cole JA., Butler CS., Butt JN., Hemmings AM., Richardson DJ. a.hemmings@uea.ac.uk,d.richardson@uea.ac.uk 17-May-2018: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro epr electron paramagnetic resonance ESR EPR EPR ESR epr predetermined predetermined participant predetermined Jepson BJ., Mohan S., Clarke TA., Gates AJ., Cole JA., Butler CS., Butt JN., Hemmings AM., Richardson DJ. a.hemmings@uea.ac.uk,d.richardson@uea.ac.uk Accepted 2018-APR-30 AT 10:42 BST AT 10:42 BST by LIVIAP The Journal of biological chemistry 2007 Only protein-protein interactions imex curation imex curation Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli. Spectropotentiometric and structural analysis of the periplasmic nitrate reductase from Escherichia coli. The Journal of biological chemistry 2007 imex curation Jepson BJ., Mohan S., Clarke TA., Gates AJ., Cole JA., Butler CS., Butt JN., Hemmings AM., Richardson DJ. a.hemmings@uea.ac.uk,d.richardson@uea.ac.uk 17-May-2018: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Jepson BJ., Mohan S., Clarke TA., Gates AJ., Cole JA., Butler CS., Butt JN., Hemmings AM., Richardson DJ. a.hemmings@uea.ac.uk,d.richardson@uea.ac.uk Accepted 2018-APR-30 AT 10:42 BST AT 10:42 BST by LIVIAP The Journal of biological chemistry 2007 Only protein-protein interactions imex curation imex curation mo(=o)-bis(molybdopterin guanine dinucleotide)(4-) Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-) Mo(=O)-bis(molybdopterin guanine dinucleotide) tetraanion Mo-bis(molybdopterin guanine dinucleotide) molybdate-bis(molybdopterin guanine dinucleotide) tetraanion small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) napb_ecoli Periplasmic nitrate reductase, electron transfer subunit Diheme cytochrome c NapB napB yejY b2203 JW5367 protein protein ecoli Escherichia coli (strain K12) MKSHDLKKALCQWTAMLALVVSGAVWAANGVDFSQSPEVSGTQEGAIRMPKEQDRMPLNYVNQPPMIPHSVEGYQVTTNTNRCLQCHGVESYRTTGAPRISPTHFMDSDGKVGAEVAPRRYFCLQCHVPQADTAPIVGNTFTPSKGYGK 6F38F13C092178AF napa_ecoli Periplasmic nitrate reductase yojC yojD yojE napA b2206 JW2194 protein protein ecoli Escherichia coli (strain K12) MKLSRRSFMKANAVAAAAAAAGLSVPGVARAVVGQQEAIKWDKAPCRFCGTGCGVLVGTQQGRVVACQGDPDAPVNRGLNCIKGYFLPKIMYGKDRLTQPLLRMKNGKYDKEGEFTPITWDQAFDVMEEKFKTALKEKGPESIGMFGSGQWTIWEGYAASKLFKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGANMAEMHPILWSRITNRRLSNQNVTVAVLSTYQHRSFELADNGIIFTPQSDLVILNYIANYIIQNNAINQDFFSKHVNLRKGATDIGYGLRPTHPLEKAAKNPGSDASEPMSFEDYKAFVAEYTLEKTAEMTGVPKDQLEQLAQLYADPNKKVISYWTMGFNQHTRGVWANNLVYNLHLLTGKISQPGCGPFSLTGQPSACGTAREVGTFAHRLPADMVVTNEKHRDICEKKWNIPSGTIPAKIGLHAVAQDRALKDGKLNVYWTMCTNNMQAGPNINEERMPGWRDPRNFIIVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVQAPGEAKSDLWQLVQFSRRFKTEEVWPEDLLAKKPELRGKTLYEVLYATPEVSKFPVSELAEDQLNDESRELGFYLQKGLFEEYAWFGRGHGHDLAPFDDYHKARGLRWPVVNGKETQWRYSEGNDPYVKAGEGYKFYGKPDGKAVIFALPFEPAAEAPDEEYDLWLSTGRVLEHWHTGSMTRRVPELHRAFPEAVLFIHPLDAKARDLRRGDKVKVVSRRGEVISIVETRGRNRPPQGLVYMPFFDAAQLVNKLTLDATDPLSKETDFKKCAVKLEKV DIP protein P33937 original sequence version: 91 DIP protein P33937 original sequence version: 102 DIP protein P33937 original sequence version: null CE2D7AB000FEAFCA tetra-mu3-sulfido-tetrairon tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) napa-napb-2 2 4 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 1D, 1E To explore further the strength of the interaction between E. coli NapA and NapB, the dissociation constant of the air-oxidized and dithionite-reduced NapA-NapB complex was measured using sedimentation equilibrium centrifugation. napa-napb-3 1 6 unspecified role unspecified role neutral component neutral component 4 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 5 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 2B In order to study the potentiometric properties of the NapA and NapB redox centers in the NapAB complex, the heteromonomers were mixed together at equimolar concentrations of 100 μm. mo(=o)_bis(molybdopterin guanine dinucleotide)(4_)-napa-1 1 3 unspecified role unspecified role neutral component neutral component 5 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 3B To investigate the properties of the E. coli NapA Mo5+ state further, EPR spectra of poised samples were collected. napa-tetra_mu3_sulfido_tetrairon-2 1 6 unspecified role unspecified role neutral component neutral component 5 unspecified role unspecified role neutral component neutral component purified purified ecoli Escherichia coli (strain K12) direct interaction direct interaction Fig. 2A The X-band EPR spectrum of air-oxidized NapA, collected at 10 K, indicated the presence of a small amount of a signal characteristic of a [3Fe-4S]1+ cluster (Fig. 2A).