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  • In his blood

    Mark Hargrove has a passion for science and music

  • At first glance Mark Hargrove's office in the Molecular Biology Building is no different from any other faculty office on campus. A computer sits humming away with a printer close by.

    Bookshelves are filled to the brim with reference materials. The desk is a little cluttered.

    But if you look closer, back in the corner sits a guitar. If biochemistry is Hargrove's first love, then music is a close second.

    "Music is fun as a compliment to what I do here," he said.

    Hargrove has been musically inclined since growing up in Lincoln, Neb. During his undergraduate and graduate studies, he took time off to play in bluegrass bands. Even at Iowa State, the assistant professor of biochemistry, biophysics and molecular biology still finds time to regularly play.

    "I wouldn't want to be a musician for a living," he said. "But it's nice to have a job that allows me the flexibility to fit in music on the side."

    That job involves his research group, which investigates structure and function of plant hemoglobins including leghemoglobin associated with nitrogen fixing bacteria and the separate family of non-symbiotic hemoglobins.

    There is little mystery to the physiological function of most human and animal hemoglobins, which are well known as the carriers of oxygen molecules in blood and muscle tissue.

    That isn't the case with hemoglobins in plant life.

    "Plants have hemoglobins, but we have no idea of their physiological roles," Hargrove said.

    Hargrove's research group is attempting to find out just what plant hemoglobin does do through his work that is funded by the National Science Foundation and the U.S. Department of Agriculture.

    "Hemoglobin is an ideal system for developing an understanding of the relationship between the structure and function of proteins," Hargrove said. "This is a fairly new research topic and a pretty hot area.

    "Furthermore, heme proteins, which are less understood physiologically and biophysically, have been discovered with what appear to have a wide variety of novel signaling and scavenging functions."

    Another new discovery made this past year of a new human hemoglobin has also spurred Hargrove's group. The new hemoglobin is very similar to the plant hemoglobin.

    "We were already doing work on the plant hemoglobin so it's just a natural extension for us to start looking at the new, similar human protein," he said.

    "This is a fairly novel class of hemoglobins," Hargrove continued. "That makes it very different from those inside your red blood cells, but there looks to be a correlation between hemoglobins in humans and all plants."

    Hargrove began work as an undergraduate at the University of Nebraska-Lincoln on soybean hemoglobin. That work continued at Rice University during his doctoral and postdoctoral work.

    "We would like to discover the function of these new hemoglobins and how their structures dictate their function," Hargrove said. "There are new hemoglobin being discovered all the time. We're trying to find the correlation between plants, bacteria and animals."

Mark Hargrove in lab

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November 5-11, 2001

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