One suggestion would be to gain more understanding of life processes. For that, we design science experiments in situ, in vitro, in vivo, and/or in modeling. There are facilities to consider like the National Synchrotron Light Source (NSLS) at Brookhaven National Laboratory (BNL) and the Advanced Photon Source (APS) at Argonne National Laboratory. You don't have to work at these laboratories to conduct experiments. Increased science funding would enhance collaborations at these sites. The reference article gives you some information about both facilities.[1]

Allen M. Orville of BNL and his collaborators from Georgia State University and University of Miami have succeeded in using the beamlines at NSLS and APS to illuminate important details about a class of enzymes that are involved widely in life processes. They
reported their findings in Biochemistry as understanding for the first time in three-dimensions what oxygen activation looks like within these enzymes. The team combined x-ray diffraction and optical absorption spectroscopy techniques into one setup.

The researchers obtained the crystals of the oxidized enzyme from its aerobic mother liquor. Then they studied the single-crystal spectroscopic properties of choline oxidase as a function of X-ray exposure.
Their "multidisciplinary experimental approach and correlation with complementary theoretical analysis thus provide direct evidence for an important oxygen intermediate in the reaction cycle of flavin-dependent enzymes." Two sets of experimental data were collected from the same crystal as evidence for the trapped reactive oxygen intermediate in choline oxidase.

Imagine what you might be able to do for your quest.


[1] Allen M. Orville, George T. Lountos, Steffan Finnegan, Giovanni Gadda, and Rajeev Prabhakar ; "Crystallographic, Spectroscopic, and Computational Analysis of a Flavin C4a−Oxygen Adduct in Choline Oxidase." Biochemistry (ACS) XXXX, xxx, 000–000 DOI: 10.1021/bi801918u;