Putidaredoxin structure

P450cam from the soil bacterium Pseudomonas putida. The availability of large quantities of this stable and soluble enzyme, and its physiological electron transport cofactor proteins putidaredoxin reductase and putidaredoxin, made possible detailed spectroscopic and mechanistic investigations into P450 catalysis. P450cam was also the first P450 enzyme to be structurally characterized. ... 

The crystal structure of NADPH-cytochrome P450 reductase (CPR), the common electron-transfer protein of Class 11 eukaryotic P450 systems, was reported in 1997. This was followed by the structures of adrenodoxin reductase (AdR) and adrenodoxin (Adx), the two electron-transfer proteins of the Class 1 mitochondrial P450 system. The crystal structure of a cross-linked AdR-Adx complex has also been reported. " Putidaredoxin reductase (PdR) and putidaredoxin (Pd) of the P450cam system have also been structurally characterized. ... 

P450cam hydroxylates Ru-Cg-Ad when supplied with electrons via the natural NADH/putidaredoxin reductase/putd reduction relay.Ru-Cg-Ad hydroxylation occurs at only 1.6% the rate of camphor hydroxylation, and only 10% of the electrons supplied by NADH go to product formation. Presumably the rest are diverted to the formation of reduced oxygen species such as superoxide or hydrogen peroxide. The remarkable ability of P450cam to hydroxylate a molecule so structurally different from camphor supports the hypothesis that the structural flexibility inherent in the P450 fold allows these enzymes to hydroxylate structurally diverse substrates. 

Another recent advance in P450 electron transfer is the solution of both the putidaredoxin (Pdx) and putidaredoxin reductase (Pdr) crystal structures. Thus, the structure of all components of the P450cam monooxygenase system now are known. The Pdx and Pdr structures are... 

Figure 3.14. Structures of the adrenodoxin (Adx)-andrenodoxin reductase (Adr) complex, putidaredoxin (Pdx), and putidaredoxin reductase (Pdr). For comparisons, the structure of glutathione reductase also is shown.

Sevrioukova, I.F., H. Li, T.L. Poulos (2004). Crystal structure of putidaredoxin reductase from pseudomonas putida, the final structural component of the P450cam monooxygenase system. J. Mol. Biol. 236, 889-902. 

Pochapsky, T, T.A. Lyons, S. Kazanis, T. Arakaki, and G. Ratnaswamy (1996). A structure-based model for cytochrome P450cam-putidaredoxin interactions. Biochimie 78, 723-733. 

H. Shimada, and I. Morishima (2003). NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin Functional significance of the putidaredoxin-induced structural changes. J. Biol. Chem. 2, 2. 

Shiro Y, lizuka T, Makino R, Ishimura Y, Morishima I (1989) N-15 NMR-Study on cyanide (C-15n-) complex of cytochrome-P-450cam-Effects of D-camphor and putidaredoxin on the iron ligand structure. J Am Chem Soc 111 7707-7711... 

Stayton PS, Sligar SG (1991) Structural micro-heterogeneily of a tryptophan residue required for efficient biological electron transfer between putidaredoxin and cytochrome P-450cam. Biochemistry 30 1845-1851... 

Hiruma Y, Hass MA, Kikui Y, Liu WM, Olmez B, Skinner SP, Blok A, Kloosterman A, Koteishi H, Lohr F, Schwalbe H, Nojiri M, Ubbink M (2013) The structure of the cytochrome p450cam-putidaredoxin complex determined by paramagnetic NMR spectroscopy and crystallography. J Mol Biol 425 4353 365... 

Shimada H, Nagano S, Ariga Y, Unno M, Egawa T, Hishiki T, Ishimura Y, Masuya F, Obata T, Hori H (1999) Putidaredoxin-cytochrome p450cam interaction. Spin state of the heme iron modulates putidare-doxin structure. J Biol Chem 274 9363-9369... 

Nagano S, Tosha T, Ishimori K, Morishima I, Pou-los TL (2004) Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding. J Biol Chem 279 42844-9... 

Fig. 6.30 P450 protein/partner complexes. A cartoon view is shown for two crystal structures documenting distinct P450 protein/partner protein interactions. Panel A depicts the P450cam (CYPIOIAI )-putidaredoxin (PD) complex with the redox partner depicted in orange (PDB 4JWS). The 2Fe-2S cluster is in close vicinity of the heme, with the PD docking on the proximal face of the P450 near to the fifth ligand cysteinate-iron bond region [770]. In contrast, panel B shows the interaction observed...

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