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| {{STRUCTURE_1jdr| PDB=1jdr | SCENE= }} | | {{STRUCTURE_1jdr| PDB=1jdr | SCENE= }} |
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| '''Crystal Structure of a Proximal Domain Potassium Binding Variant of Cytochrome c Peroxidase'''
| | ===Crystal Structure of a Proximal Domain Potassium Binding Variant of Cytochrome c Peroxidase=== |
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| ==Overview==
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| Earlier work [Bonagura et al. (1996) Biochemistry 35, 6107] showed that the K+ site found in the proximal pocket of ascorbate peroxidase (APX) could be engineered into cytochrome c peroxidase (CCP). Binding of K+ at the engineered site results in a loss in activity and destabilization of the CCP compound I Trp191 cationic radical owing to long-range electrostatic effects. The engineered CCP mutant crystal structure has been refined to 1.5 A using data obtained at cryogenic temperatures which provides a more detailed basis for comparison with the naturally occurring K+ site in APX. The characteristic EPR signal associated with the Trp191 radical becomes progressively weaker as K+ is added, which correlates well with the loss in enzyme activity as [K+] is increased. These results coupled with stopped-flow studies support our earlier conclusions that the loss in activity and EPR signal is due to destabilization of the Trp191 cationic radical.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10220341}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10220341 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10220341}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Sundaramoorthy, M.]] | | [[Category: Sundaramoorthy, M.]] |
| [[Category: Helical bundle protein]] | | [[Category: Helical bundle protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:06:03 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:05:12 2008'' |