We have designed a simple protein, monomeric four-α-helix bundle, which can serve as a platform for diverse set of oxidoreductase related functions. We describe the progressive design steps taken from the simplest α-helical peptide toward functionalized proteins. This platform has considerable latitude for external charge patterning and internal control of stability, both globally and locally. We show how ligation of photoactive and redox cofactors can induce the stabilization and structuring of helices. We demonstrate that this platform can accomplish not one, but variety of functions, including electron transfer to natural proteins, O2 binding sustained for seconds, CO and NO sensing, millisecond superoxide bursts and triplet-excited state-driven nanosecond charge-separation followed by micro to millisecond electron tunneling reactions. We will present our strategies for optimizing bacterial expression, assembly of natural cofactors such as hemes, flavins, iron-sulfur clusters, quinone, nicotinamide and light active cofactors (porphyrins, chlorins) and many more synthetic analogues with a control over the distance and orientation that allow tuning for specific selected function. These maquette proteins can be altered to assemble in water, membranes and on a range of surfaces including titania. Such versatility makes this protein platform suitable for further iterative designs for light energy harvesting, photochemical charge separation, oxygen transport, oxidative metabolism as well as understanding of fundamental properties of enzyme activity, stability, and folding.