Henry A. Charlier, Jr.                                                               
Associate Professor
hcharlier@chem.boisestate.edu
SN 311
208-426-3474

Education

1986-1991 B.S. Chemistry and Biology - University of Wisconsin-Stevens Point, Stevens Point, WI
1991-1996 Ph.D. Biochemistry - Medical College of Wisconsin, Milwaukee, WI
1997-2000 Postdoc Biochemistry - University of Iowa, Iowa City, IA

About Me

Chemistry and Outreach: Even though chemistry is my vocation, it is also my hobby. I love to do chemistry demonstrations. I am always amazed by what I see.  I am very active in sharing my love of chemistry with the community, often times as my alter ego Dr. Picklestein.  To learn more about my outreach efforts and those of the Department of Chemistry and Biochemistry at Boise State University, click here.

  Idaho Academy of Science: I am the president of the Idaho Academy of Science (IAS).  This year marks the 50^th anniversary of the IAS and this Spring we celebrate the 50^th anniversary at our 50^th Annual Meeting to be held in Boise and hosted by Boise State University and the College of Western Idaho.  The dates of the meeting are March 27 - 29, 2008.  To learn more about the meeting, register and/or submit an abstract for the meeting click here.

Fishing: I am an avid fisherman. My favorite style of fishing is fly fishing and my most productive fly is a #10 black woolybugger with brown hackle. It catches everything from trout to bass to bluegill. I love to fish Idaho, Iowa, and Wisconsin. This woolybugger is effective in each state. I should mention that I also love to fish with muddler minnows. I have used this fly to catch nearly all species of trout and in Wisconsin have caught both smallmouth bass and walleyes.  I even caught a catfish with it.  My other productive flies include the cattertail, stayner ducktail, and stimulator.  Check out some of my favorite catches.

Photography:  I have recently obtained a digital SLR camera and have been enjoying learning to take pictures.  See my favorites taken to this point.

Collegiate Wrestling:  Ever since my time at Iowa, I have been an avid collegiate wrestling fan.  Boise State has an excellent wrestling program and offers some of the most exciting sporting events on campus.  For a list of links that provide information about Boise State Wrestling click here or check out our Boise State Athletics website.

Pets: I have variety of pets that include a dog, guinea pig, milk snake, king snake, Russian tortoise, 3 gerbils, 2 parakeets, and 4 zebra finches.

My Brother Matt: I have two brothers and two sisters.  My brother Matt has a striking resemblance to me and he is also has a very similar sense of humor.  One really bad combination is when I have a camera and he has the urge to model.  I thought that I would provide a few examples of his modeling.  The other person in some of these pictures is my best friend Jeff Schilling.  Jeff is a freelance writer for a hunting magazine.  Click to see the insanity: Matt1, Matt2, Matt3, Matt4, Matt5, Matt6, Matt7.

Teaching Philosophy

I believe that students need to take responsibility for their own learning and my role is to be more of a learning coach than a lecturer. I try to provide opportunities for students to experience the material rather than to simply hear a lecture and memorize material. In my experience as a teacher and a student, I have found that if I haven’t developed an understanding of the fundamentals, I never learned the material and have forgotten it. My other belief is that one should work hard and play hard. I always try to build fun into the classroom, while at the same time I work hard to challenge each student and help them to achieve goals that they may not have thought possible.

Research

My overall research interests involve the fields of enzymology and protein chemistry. Proteins are very interesting molecules that serve a variety of functions in living organisms. My current research involves studies in three areas as briefly described below:

Carbonyl Reductase - Carbonyl reductase (CR), E.C. 1.1.1.184, catalyzes the NADPH-dependent reduction of a wide range of carbonyls. CR has been connected to several important processes including but not limited to quinone detoxification, neuroprotection, prostaglandin metabolism, and, of clinical interest, anthracycline metabolism. CR reduction of anthracyclines significantly impacts their use in the treatment of cancer as it has been linked to both drug resistance and cardiotoxicity mechanisms. Therefore, inhibition of CR in conjunction with anthracycline therapy offers the potential both to increase the effectiveness of the drugs and to decrease the risk of the associated cardiotoxicity. The major emphasis of this work is to better understand how CR recognizes the molecules to which it binds, be they substrates or inhibitors. Equipped this information, drugs may be designed to control CR with the intention of reducing the risk of cardiotoxicity during anthracycline cancer treatment. Also, as the role of CR is other pathways is better understood such drugs may be used to treat other diseases as well. Pictured ar right: Structure of human carbonyl reductase. From http://www.rcsb.org/pdb/explore/explore.do?structureId=1WMA

Alcohol Dehydrogenase - Alcohol dehydrogenase (ADH), E.C. 1.1.1.1, catalyzes the reversible oxidation of ethanol, using NAD as a cofactor. This reaction is a rate-limiting step in alcohol metabolism. ADH may be an important determinant in the development of alcoholism and fetal alcohol syndrome and is therefore widely studied. In addition, it often studied to gain insight into how enzymes catalyze reactions. My research project with ADH focuses on evaluating the contribution of electrostatic interactions in coenzyme binding. In past studies, a lysine at position 228 (K228) has been implicated in controlling, at least in part, coenzyme (NAD+ and NADH) binding. In particular, the positive charge at this position is hypothesized to interact with the negatively charged coenzymes. In order to evaluate the role of charge at position 228, we mutated the lysine at this position to alanine, glutamine, and glutamate, each of which changes the charge at this position. In a past study this lysine was also mutated to arginine, which conserves the positive charge at 228. Currently, all of these mutants are being analyzed for effects on coenzyme binding using steady state and transient kinetics, equilibrium binding studies, and computational chemistry. Pictured at left: Structure of horse liver alcohol dehydrogenase. From http://www.rcsb.org/pdb/explore.do?structureId=1HLD

Phosphotriesterase – Phosphotiesterase (PTE), E.C. 3.1.8.1, catalyzes the hydrolysis of synthetic organophosphate triesters and phosphorofluoridates. Compounds in this family include several pesticides and nerve agents. This enzyme has potential use in nerve agent and pesticide decontamination. Work in my lab involves using protein chemistry and genetic engineering techniques to modify this enzyme to enhance its utility in organophosphate compound degradation. Pictured at right: Structure of bacterial phosphotriesterase. From http://www.rcsb.org/pdb/explore/explore.do?structureId=1P6C