Cytochrome P450 reductase structure

Huang WC, Ellis J, Moody PC, Raven EL, Roberts GC (2013) Redox-linked domain movements in the eatalytie eycle of cytochrome P450 reductase. Structure 21 1581 1589... 

D. Active Site Environment Human HO-1 Crystal Structure Interaction with Cytochrome P450 Reductase Gaseous Ligands... 

Wang, M., Roberts, D. L., Paschke, R., Shea, T. M., Masters, B. S., and Kim, J. J., 1997, Three-dimensional structure of NADPH-cytochrome P450 reductase prototype for FMN- and FAD-containing enzymes Proc. Natl. Acad. Sci. U. S. A. 94 8411n8416. 

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. ... 

Figure 7 The crystal structure of NADPH-cytochrome P450 reductase (CPR). The FAD and FMN domains are linked by a hinge domain...

Black, S.D. and M.J. Coon (1982). Structural features of liver microsomal NADPH-cytochrome P450 reductase hydrophobic domain, hydrophilic domain and connecting region. J. Biol. Chem. 257, 5929-5938. 

Fig. 25.5. General structure of cytochrome P450 enzymes. O2 binds to the P450 Fe-heme in the active site and is activated to a reactive form by accepting electrons. The electrons are donated by the cytochrome P450 reductase, which contains an FAD plus an FMN or Fe-S center to facilitate the transfer of single electrons from NADPH to O2. The P450 enzymes involved in steroidogenesis have a somewhat different structure. For CYP2E1, RH is ethanol (CH3CH2OH) and ROH is acetaldehyde (CH3COH).

Only a few years ago, the crystallisation and structure elucidation of human placental aromatase has been achieved (Fig. 6.9). [14] Now, it became possible to gain a deeper understanding of how the enzyme operates and why it has such a high substrate selectivity - in contrast to many other cytochrome P450 reductases. 

Both NADPH cytochrome P450 reductase (P450 reductase) and NAD(P)H-quinone oxidoreductase (NQO) are flavin adenine nucleotide-containing enzymes that catalyze the reduction of quinones and quinone-like structures. However, P450 reductase is a microsomal enzyme that catalyzes a one-electron reduction to yield semiquinone radieals that can redox cycle to produce superoxide anion radicals, whereas NQO is a cytosolic enzyme that catalyzes a two-electron reduction to yield hydroquinones (Matsunaga et al., 2006). P450 reductase also can catalyze the one-electron reduction of nitroaromatics to the nitro anion radical, which can redox cycle ... 

Strobel HW, Hodgson AV, Shen SJ (1995) NADPH cytochrome P450 reductase and its structural and... 

Narayanasami R, Horowitz PM, Masters BS (1995) Flavin-binding and protein structural integrity studies on NADPH-cytochrome P450 reductase are consistent with the presence of distinct domain. Arch Biochem Biophys 316 267-274... 

Zhao Q, Modi S, Smith G, Paine M, McDonagh PD, Wolf CR, Tew D, Lian LY, Roberts GC, Driessen HP (1999) Crystal structure of the FMN-binding domain of human cytochrome P450 reductase at 1.93 A resolution. Protein Sci 8 298-306... 

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