Azotobacter vinelandii nitrogenase protein

Dean, D.R., Setterquist, R.A., Brigle, K.E., Scott, D.J., Laird, N. F., Newton, W.E., (1990) Evidence that conserved residues Cys-62 and Cys-154 within the Azotobacter vinelandii nitrogenase iron-molybdenum protein a-subuflit are essential for nitrogenase activity but conserved residues His-83 and Cys-88 are not. Mol. Microbiol. 4(9),... 

Watt, G.D. and Reddy, K.R.N. (1994) Formation of an all ferrous Fe4S4 cluster in the iron protein-component of Azotobacter vinelandii nitrogenase, J. Inorg. Biochem. 53, 281-294. 

A) Preliminary x-ray crystal structure of the Azotobacter vinelandii nitrogenase Fe protein. ... 

In late 1992 the first crystal structures of the Fe and MoFe proteins of Mo nitrogenase frora Azotobacter vinelandii were published (1-3). 

The nitrogenase proteins are generally characterized by two letters indicating the species and strains of bacteria and the numerals 1 for the MoFe protein and 2 for the Fe protein. Thus, the Fe protein from Azotobacter vinelandii is Av2 and the MoFe protein from Klebsiella pneumoniae is Kpl. 

Figure 31 X-Ray structure of the active site of Fe-protein in the nitrogenase of Azotobacter vinelandii. Polypeptide chains surround the central Fe4S4 cluster...

Recently, a second or alternative nitrogenase has been isolated from Azotobacter vinelandii (21) and Azotobacter chroococcum (22) that contains vanadium as opposed to molybdenum. The MoFe and VFe nitrogenase proteins from A. vinelandii (called Av and. 4vl , respectively) are known to have different polypeptide structures and it obviously of interest to know to what extent the cluster composition is conserved. Variable temperature MCD studies of the as isolated and thionine oxidized proteins provided a convenient means of addressing this question. 

Georgiadis, M.M., Komiya, H., Chakrabarti, P., Woo, D., Komuc, J.J., Rees, D.C. (1992). Crystallographic structure of the nitrogenase iron protein from Azotobacter Vinelandii. Science 257, 1653-1659. 

The Fe proteins of all three nitrogenases are very similar [1], The Fe protein of Mo nitrogenase is a dimer (Mr —65,000) of equivalent subunits with a single Fe4S4 cluster bound between the subunits by bonds between the cluster Fe atoms and the S atoms of two cysteine residues from each subunit [2], The x-ray crystallographic structure at 0.29 nm resolution of the Fe protein from Azotobacter vinelandii (Av2) has been described (Figure 1) [6], This shows that the Fe4S4... 

The biosynthesis of Fe/S clusters may well proceed via other, possibly more simple Fe/S clusters as intermediates. The products of the genes riifS and nif U in Azotobacter vinelandii are thought to collaborate in nitrogenase metal-locluster biosynthesis NIFS is a sulfide donor NIFU is a [2Fe-2S] protein. The... 

Figure 10.3 Crystallographic structures of the most important iron-sulphur centres in proteins (a) dimeric centre of ferrodoxin from Spinacia oleracea [54], (b) trimeric centre of ferredoxin from Bacillus schlegelii [55], (c) cubane cluster of nitrogenase reductase from Azotobacter vinelandii [56], (d) nitrogenase octameric cluster from Azotobacter vinelandii [57], (e) nitrogenase octameric cluster from Clostridium pasteurianum [58], (f) MoFe cluster of nitrogenase from Azotobacter vinelandii [59], and (g) active centre of sulphite reductase from Escherichia coli [60]...

Strop P,Tatahara PM, Chiu H-J, Angove HC. Crystal structure of the all-ferrous [4Fe-4S]° form of the nitrogenase iron protein from Azotobacter vinelandii. Biochemistry 2001 40 651-6. 

The principle advances in the area has been made using x-ray structural analysis. Crystallographic data have been first produced for the nitrogenase complex of FeP (A2) and FeMoP (Al) from Azotobacter vinelandii (Kim and Rees, 1992) and for the corresponding complex of Cp2 and Cpl from Clostridium pasterianum (Bolen et al., 1993), ). A 1.6 A resolution X-ray crystallographic structure of Klebsiella pneumoniae proteins has been recently reported (Mayer et al., 1999) It was shown that FeMoco sites in Al, Cpl, and Kpl are 70 A apart and FeMoco and P clusters are separated by about 19 A. X-ray structures of the nitrogenase complex and the active site clusters are presented in (Figs. 3.2-3.4). 

DeRose, V.J. C.-H., Kim, W.E., Newton, D. R.D., and Hoffman B. M. (1995) Electron Spin Echo Modulation Spectroscopic Analysis of Altered Nitrogenase MoFe Proteins of Azotobacter vinelandii, Biochemistry 34, 2809-2814... 

Duyvis, M. G., Wassink, H., and Haaker, H. (1998) Nitrogenase of Azotobacter vinelandii kinetic analysis of the Fe protein cycle, Biochemistry 37, 17345-17354. 

Kim, J. and Rees, D.C. (1992) Crystallographic structure and functional implication of the nitrogenase molybdenum-iron protein from Azotobacter vinelandii, Nature 360, 556-560. 

The two nitrogenase proteins, Fe-protein and MoFe-protein, are composed of a total of three different types of subunits and contain three different types of metal centers. The properties of the nitrogenase proteins have been extensively studied and are summarized below. To distinguish the two nitrogenase proteins isolated from different bacterial sources, the MoFe-protein and Fe-protein are designated as components 1 and 2, respectively, preceded by a two-letter abbreviation of the source species and genus i.e., Avl is MoFe-protein isolated from Azotobacter vinelandii and Cp2 is Fe-protein isolated from Clostridium pasteurianum, etc. 

M.M. Georgiadis, H. Komiya, P. Chakrabarti, D. Woo, J.J. Komuc, and D.C. Rees. 1992. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii Science 257 1653-1659. (PubMed)... 

Figure 2.32. Nitrogenase Mo-Fe protein from Azotobacter vinelandii. Hydrogen and amino acid atoms are not shown. Based on Protein Data Bank ID IMlN (Einsle et al, 2002). There are four sets of FegS and MoFe7S9N clusters, with one enlarged in Fig...

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