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Azotobacter vinelandii
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== Nitrogenase == The [[nitrogenase]] [[enzyme|holoenzyme]] of ''A. vinelandii'' has been characterised by [[X-ray crystallography]] in both [[Adenosine diphosphate|ADP]] tetrafluoroaluminate-bound<ref>{{cite journal | vauthors = Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC | year = 1997 | title = Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction | journal = Nature | volume = 387 | issue = 6631 | pages = 370β376 | doi=10.1038/387370a0| pmid = 9163420 | s2cid = 1582534 }}</ref> and Mg[[Adenosine triphosphate|ATP]]-bound<ref>{{cite journal | vauthors = Chiu H, Peters JW, Lanzilotta WN, Ryle MJ, Seefeldt LC, Howard JB, Rees DC | year = 2001 | title = MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127 Delta-Fe-protein and the MoFe-protein | journal = Biochemistry | volume = 40 | issue = 3 | pages = 641β650 | doi=10.1021/bi001645e| pmid = 11170380 }}</ref> states. The enzyme possesses [[molybdenum]] [[iron]]-[[sulfido]] cluster [[Cofactor (biochemistry)|cofactors]] ([[FeMoco]]) as [[active site]]s, each bearing two pseudocubic iron-sulfido structures.
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