Microbial biosynthesis cytochromes

Table 1 collects selected metric parameters and IR stretching frequencies (wno) fot a representative set of six-coordinated (6C) complexes of iron, ruthenium, and osmium, and few iron 5C-compounds. A number of Fe(III) heme proteins are involved in the regulation of the NO biosynthesis by the enzyme NO synthase, in NO transport (as vasodilator) in nitrophorins and in NO inhibition processes of cytochrome P450 and related enzymes (45). Heme enzymes are also intermediates in cyt cd nitrite reductases (NIRs), (46) and in NO reduction by a fungal cyt P450 NO reductase (47). The nonheme Fe(III) nitrile hydratase enzyme (NHase) is relevant to the microbial assimilation of organic nitriles, using... 

First, Ro and Douglas constructed the initial steps of the plant phenylpropanoid pathway by connecting two enzymes, PAL and C4H, with a cytochrome P450 reductase (CPR) from a plant source in S. cerevisiae [31]. This heterologous transfer of plant phenylpropanoid pathway genes into yeast became the platform for the biosynthesis of various flavonoids and related compounds in microbial... 

Cytochrome P-450s are the best-known class of hydroxylation enzyme. Their active sites contain a heme iron that forms a highly activated oxygenating species that reacts by a radical mechanism. In higher animals, they function primarily in metabolite degradation as part of pathways that clear unnatural substances such as toxins and drugs. Hydroxylation inaeases polarity that facilitates further derivatization by other detoxification enzymes or excretion of the hydroxylated products. Other P-450 family members are involved in secondary metabolite biosynthesis, particularly in plants and microbial cells (Figure 1.6). 

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