Accumulating evidence indicates that there is a multiplicity of cytochrome P-450 enzymes in plants. These monooxygenases are implicated in the metabolism of sterols, terpenes, gibberellins, isoflavonoids, and xenobiotics. Evidence that cytochromes P-450 are involved in the detoxification of herbicides (chlorotoluron, primsulfuron, and diclofop) includes photoreversible CO inhibition of the reactions, and a requirement for 02 and NADPH. Several cytochromes P-450, Mr 45,000 to 65,000, have been isolated, including hydroxylases of cinnamic acid, 3,9-dihydroxypterocarpan, and digitoxin. In some cases the purified cytochrome P-450 has been successfully reconstituted with NADPH:cytochrome P-450 reductase (Mr 72,000-84,000 protein). This reductase appears to be a nonspecific electron donor to different forms of cytochrome P-450. Immunological techniques and specific inhibitors (triazoles, imidazole derivatives) are being used to characterize plant cytochromes P-450 and the NADPH:cytochrome P-450 reductase. Specific cytochromes P-450 are induced by wounding or pathogens, others are expressed in specific cell types. Plant cytochromes P-450 are found in various subcellular locations, including endoplasmic reticulum, plasma membranes, glyoxysomes, and perhaps mitochondria. A cytochrome P-450 demethylase from avocado has recently been sequenced and found to have a hydrophobic N terminus similar to the membrane anchor of cytochromes P-450 from other organisms. The existence of cytochromes P-450 in different subcellular locations suggests that there are many genes for cytochromes P-450 in plants which have yet to be identified and classified.Cyt P-450 are membrane-bound heme-containing proteins which have been implicated in a variety of oxidative reactions in plant tissues. A wide range of reactions are mediated by specific forms of these proteins. Cyt P-450-linked enzymes have been implicated in biosynthetic pathways leading to the synthesis of lignin phenolics, membrane sterols, phytoalexins, and terpenoids (33). It has been postulated that plants have evolved highly specific Cyt P-450-linked secondary pathways to produce defense-related phytoalexins, while animals have evolved parallel less specific, Cyt P-450-linked systems to detoxify ingested phytoalexins and other xenobiotics (11,22 at the expense of the 450 nm peak (25). For this reason the CO-hemoprotein adduct with the 420 nm peak, termed P-420, is often considered to be a degradation product of Cyt P-450.In addition to the nonspecific inhibition by CO, certain Cyt P-450 activities are selectively inhibited by various imidazole, pyrimidine, and triazole derivatives. Inhibitor binding also can be determined spectrophotometrically by changes in difference spectra. A typical Cyt P-450 spectrum of any mem-669 www.plantphysiol.org on May 10, 2018 -Published by Downloaded from