<p>Abstract</p> <p>Background</p> <p>Membrane proteins are an important class of proteins, playing a key role in many biological processes, and are a promising target in pharmaceutical development. However, membrane proteins are often difficult to produce in large quantities for the purpose of crystallographic or biochemical analyses.</p> <p>Results</p> <p>In this paper, we demonstrate that synthetic gene circuits designed specifically to overexpress certain genes can be applied to manipulate the expression kinetics of a model membrane protein, cytochrome <it>bd </it>quinol oxidase in <it>E. coli</it>, resulting in increased expression rates. The synthetic circuit involved is an engineered, autoinducer-independent variant of the <it>lux </it>operon activator LuxR from <it>V. fischeri </it>in an autoregulatory, positive feedback configuration.</p> <p>Conclusions</p> <p>Our proof-of-concept experiments indicate a statistically significant increase in the rate of production of the <it>bd </it>oxidase membrane protein. Synthetic gene networks provide a feasible solution for the problem of membrane protein production.</p