Nitrite reductase structure

Cytochrome cdi Nitrite Reductase Structure Raises Interesting Mechanistic Questions... 

Figure 6. Structural relationships between ascorbate oxidase, ceruloplasmin, nitrite reductase, and blood clotting factor VIII.

Figure 14.1 (Left) X-ray structure of plastocyanin from poplar leaves as a ribbon diagram with the metal ion and its ligands highlighted, PDB code 1PLC (right) Type 1 Cu site in Cu(II)-nitrite reductase from Alcaligenes faecalis, PDB code 1AS6. (From Messerschmidt et al., 2001. Reproduced with permission from John Wiley Sons., Inc.)...

STRUCTURE AND ENZYMOLOGY OF TWO BACTERIAL DIHEME ENZYMES CYTOCHROME cd NITRITE REDUCTASE AND CYTOCHROME c PEROXIDASE... 

Fig. 3. The X-ray crystal structure of the oxidized state of c3itochrome cdi nitrite reductase from P. pantotrophus (drawn from PDB entry 1 qks using MolScript 98, 99)).

Since HA is unstable in vivo , and is known to rapidly associate with the heme part of heme proteins , and possibly also with a variety of biological oxidants, such as the superoxide anion that is produced by many mammalian cells, it is difficult to demonstrate its accumulation in vivo. Already in 1932 Lindsey and Rhines discussed some analytical difficulties in the detection of HA, since when added externally, it disappeared rapidly from bacterial cultures this led to the conclusion that even if it is produced as an intermediate, its consumption is too fast to allow the accumulation of sufficient quantities for analytical demonstration. Compelling indirect evidence for the presence of HA as an intermediate in the enzymatically catalyzed reduction of nitrite (N02 ) to NH3 was provided by Einsle and colleagues , who characterized the crystal structure of the complex obtained by soaking cytochrome c-nitrite reductase with NH20H. ... 

There are a number of excellent sources of information on copper proteins notable among them is the three-volume series Copper Proteins and Copper Enzymes (Lontie, 1984). A review of the state of structural knowledge in 1985 (Adman, 1985) included only the small blue copper proteins. A brief review of extended X-ray absorption fine structure (EXAFS) work on some of these proteins appeared in 1987 (Hasnain and Garner, 1987). A number of new structures have been solved by X-ray diffraction, and the structures of azurin and plastocyanin have been extended to higher resolution. The new structures include two additional type I proteins (pseudoazurin and cucumber basic blue protein), the type III copper protein hemocyanin, and the multi-copper blue oxidase ascorbate oxidase. Results are now available on a copper-containing nitrite reductase and galactose oxidase. 

With the structure of ascorbate oxidase in hand, a new structurally based alignment of the sequences of ascorbate oxidase, laccase, and ceruloplasmin has been performed (Messerschmidt and Huber, 1990). In brief, while gene triplication for ceruloplasmin is still revelant, its sequence can be further subdivided into two domains per unit of triplicated sequence, or six domains in total. Each of these sequences bears some resemblance to each of the three domains of ascorbate oxidase, as does each of the two domains in laccase. The coppers of the trinuclear site of ceruloplasmin then are predicted to be bound between domains 1 and 6, with a type I site also lying in both domains 6 and 4 (see Huber, 1990). The relative orientation of each of these domains is not predicted by this alignment, but it turns out that the structure of nitrite reductase may shed some light on this (see Section V,C). 

Jiingst, A., Braun, C., and Zumft, W. G. (1991a). Close linkage in Pseudomonas stutzeri of the structural genes for respiratory nitrite reductase and nitrous oxide reductase, and other essential genes for denitrification. Mol. Gen. Genet. 225, 241-248. 

Sano, M., and Matsubara, T. (1988). Structural change in the one-electron oxidation-reduction at the copper site in nitrite reductase. Evidence from EXAFS. Inorg. Chem. Acta Bioinorg. Chem 152, 53-54. 

Ye, R. W., Fries, M. R., Bezborodnikov, S. G., Averill, B. A., and Tiedje, J. M. (1993). Characterization of the structural gene encoding a copper-containing nitrite reductase and homology of this gene to DNA of other denitrifiers. Appl. Environ. Microbiol. 59,... 

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