Another new concept that Shelnutt's research has revealed is that many hemes change shape and go from one distortion to another as they perform their work. For example, when a certain protein binds with oxygen, the heme in the protein changes shape, loosing its ruffling distortion. This causes the protein itself to change shape, turning off a biochemical reaction called nitrogen fixation. Then, when oxygen is no longer around, the heme ruffles once again, and nitrogen fixation is switched back on.
"Sometimes, though, the heme doesn't change at all," Shelnutt says. "It just depends on the job that needs to be done."
Shelnutt's interest in protein analysis and hemes dates back about ten years when he was researching the prospect of engineering molecules to, for example, change gaseous fuel to liquid fuel. Having a history of working with heme proteins at Bell Labs, he wondered if a protein could alter the heme's shape and function as well.
Shelnutt believes that his discovery might lead to changes in the way diseases are treated in the future or for other scientific advances. In collaboration with a French scientist, he is already using his knowledge to develop new anti-inflammatory drugs.
Another possibility is to understand how hemes from another protein Shelnutt is working with convert sulfites or nitrites -- common pollutants -- into hydrogen sulfide or ammonia. Then, analogous arrangements of hemes could be chemically engineered, produced in batches, and released to clean up waste sites.
"The revelation that heme shape is correlated to a protein's function is so new that we don't yet know where this knowledge can take us," Shelnutt says. "We have a new key to better understand life and now we have to figure out what to do with it."