Most well studied heme proteins (globins, c-and b-type cytochromes, peroxidases, P450) all have exactly the same heme prosthetic group yet each exhibits very different and very clearly defined functions. These differences are dictated by interactions between the protein and heme much of which has been deciphered through a variety of spectral probes and x-ray crystallography. The research in this proposal will center on testing hypotheses derived primarily from heme enzyme crystal structures. One question centers on the role that amino acid radicals play in peroxidase catalysis and how the protein environment helps to stabilize a particular Trp radical in cyctohrome c peroxidase. Other questions center on alternate binding sites for peroxidase substrates and mechanisms of inter-protein electron transfer. The primary methods to be employed are protein engineering coupled with crystallography and other biophysical approaches such as EPR spectroscopy and flash photolysis methods for following rapid reactions.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM042614-17
Application #
7210603
Study Section
Metallobiochemistry Study Section (BMT)
Program Officer
Ikeda, Richard A
Project Start
1989-07-01
Project End
2009-03-31
Budget Start
2007-04-01
Budget End
2008-03-31
Support Year
17
Fiscal Year
2007
Total Cost
$268,952
Indirect Cost
Name
University of California Irvine
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
046705849
City
Irvine
State
CA
Country
United States
Zip Code
92697
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Sundaramoorthy, Munirathinam; Gold, Michael H; Poulos, Thomas L (2010) Ultrahigh (0.93A) resolution structure of manganese peroxidase from Phanerochaete chrysosporium: implications for the catalytic mechanism. J Inorg Biochem 104:683-90

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