Flavin mononucleotide representation

Figure 3 Schematic representation of nitric oxide synthase isoforms and cytochrome P450 reductase. Haem, heme PDZ, PDZ domain (GLGF repeats) CaM, calmodulin FMN, flavin mononucleotide FAD, flavin adenine dinucleotide (adapted from Hobbs et al., 1999).

Fig. 5. Schematic representation of the structure of a flavocytochrome 62 subunit. A, The heme domain B, the flavodehydrogenase domain C, the C-terminal tail D, the hinge region linking the two domains E, the proteolytically sensitive loop F, flavin mononucleotide G, protoheme IX.

Fig. 2.5 Top panel, a Model of a complex between P450 and NADPH-cytochrome P450 oxidoreductase (FOR). A complex of P450 (red) and Mol A of the hinge-deletion mutant of POR(ATGEE), denoted as PORT e [53]). the flavin mononucleotide (FMN) domain (blue) and flavin adenine dinucleotide (FAD) domain (yellow)] and an enlarged view showing the relative orientation of the EMN and heme, b and c Open-book representation of molecular surface at the interface of P450 (b) and the EMN domain of POR (c). Five salt-bridge pairs are shown with same let-...

Fig. 2.6 A cartoon representation of a model for POR-P450 complex formation in the endoplasmie reticulum (ER) membrane. Flavin mononucleotide (FMN) domain, flavin adenine dinueleotide FAD) domain, and P450s are shown in blue, yellow, and red balls, respeetively. (1) Multiple P450s exist in the ER membrane. Nucleotide binding favors formation of the elosed form, similar to the one found in the erystal strueture [36]. (2) Upon binding to pyridine nueleotide (NADPH), the enzyme adopts the elosed form. In the elosed form, hydride transfer, inter-...

It has been argued that this is a free radical-type process using a flavin mononucleotide (FMN) that is reduced in the process (FMNH2). A representation of the pathway is shown in Scheme 11.83. 

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See also in sourсe #XX -- [ ]

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