Fig. 3 Light dependency of the C. variabilis alkane synthase.

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Fig. 3 Light dependency of the C. variabilis alkane synthase. Light dependency of the C. variabilis alkane synthase. (A) Absorption spectrum and action spectrum of the purified enzyme. Mean ± SD (n = 3 repeats). The position of the flavin absorption maximum in the enzyme (467 nm) deviates from typical values (445 to 450 nm for most flavoproteins and free flavins). (B) Activity of the purified enzyme under successive light conditions. Activity on 1-13C-palmitate was monitored via release of 13CO2 by using membrane inlet mass spectrometry. (C) Dependence of the activity of the purified enzyme on white light intensity. Mean ± SD (n = 3 repeats). (D) Variation of total hydrocarbons in C. reinhardtii cells grown in a photobioreactor under blue and then red light. Mean ± SD (n = 3 repeats). FAMEs, fatty acid methyl esters. Damien Sorigué et al. Science 2017;357:903-907 Copyright © 2017, American Association for the Advancement of Science