Metal halide perovskites are emerging as attractive materials for light-emitting diode (LED) applications. The external quantum efficiency (EQE) has experienced a rapid progress and reached over 21%, comparable to the state of the art organic and quantum dot LEDs. For metal halide perovskites, their simple solution-processing preparation, facile band gap tunability, and narrow emission line width provide another attractive route to harness their superior optoelectronic properties for multicolor display applications. In this work, we demonstrate a high-resolution, large-scale photolithographic method to pattern multicolor perovskite films. This approach is based on a dry lift-off process which involves the use of parylene as an intermediary and the easy mechanical peeling-off of parylene films on various substrates. Using this approach, we successfully fabricated multicolor patterns with red and green perovskite pixels on a single substrate, which could be further applied in liquid crystal displays (LCDs) with blue backlight. Besides, a prototype green perovskite micro-LED display under current driving has been demonstrated.

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Heme oxygenase catalyzes the regiospecific oxidation of hemin to biliverdin IXalpha with concomitant liberation of CO and iron by three sequential monooxygenase reactions. The alpha-regioselectivity of heme oxygenase has been thought to result from the regioselective oxygenation of the heme alpha-meso position at the first step, which leads to the reaction pathway via meso-hydroxyheme IXalpha and verdoheme IXalpha intermediates. However, recent reports concerning heme oxygenase forming biliverdin isomers other than biliverdin IXalpha raise a question whether heme oxygenase can degrade meso-hydroxyhemin and isomers other than the alpha-isomers. In this paper, we investigated the stereoselectivity of each of the two reaction steps from meso-hydroxyhemin to verdoheme and verdoheme to biliverdin by using a truncated form of rat heme oxygenase-1 and the chemically synthesized four isomers of meso-hydroxyhemin and verdoheme. Heme oxygenase-1 converted all four isomers of meso-hydroxyhemin to the corresponding isomers of verdoheme. In contrast, only verdoheme IXalpha was converted to the corresponding biliverdin IXalpha. We conclude that the third step, but not the second, is stereoselective for the alpha-isomer substrate. The present findings on regioselectivities of the second and the third steps have been discussed on the basis of the oxygen activation mechanisms of these steps.