Abstract. The alkene oxygenase (AO) of fababean (Viciafaba L.) converts ethylene to ethylene oxide. Treatment of fababeans with I0 pA/liter ethylene increases the activity of this enzyme within 2 hours of ethylene treatment. Though other alkenes were taken up by fababean seedlings, ethylene was the most active in inducing AO activity. The ability of ethylene to increase AO was blocked 60% by cycloheximide, an inhibitor of protein synthesis, and 35% by AgNO 3, an inhibitor of ethylene action.Alkene oxygenase (AO) oxidizes ethylene to ethylene oxide. Similar enzymes occur in the actinomycete, Mycobacterium paraffinicum (De Bont 1975, De Bont and Albers 1976, De Bont et al. 1979, De Bont and Harder 1978, Wiegant and De Bont 1980, animals (Ehrenberg et al. 1977, Filser andBolt 1983), and plants (Beyer 1975, Beyer 1977, Beyer 1979a, Beyer 1979b, Beyer 1980, Beyer and Blomstrom 1979, Beyer and Sundin 1978, Dodds and Hall 1982, Dodds et al. 1979, Jerie and Hall 1978. In M. paraffinicum, the function of ethylene oxidation is to provide energy and carbon for the growth of this soil-inhabiting organism. Since this enzyme lacks substrate specificity and removes a number of alkenes from the surroui~ding gas phase, the generalized name of alkene oxygenase is used in this paper. However, ethylene is probably the major alkene available to plants or actinomycetes. The description of in vivo alkene consumption as an oxygenase is based on the reports that ethylene oxide is the end product of the reaction (Dodds et al. 1979) and that the activity of the enzyme was lost in a nitrogen gas phase (Abeles 1984). However, we have not shown that molecular oxygen was incorporated directly into the alkenes used in this study. The term AO then is used here with this understanding and as a convenient way to describe the ability of V. faba to metabolize ethylene and other alkenes.