2cep
From Proteopedia
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|PDB= 2cep |SIZE=350|CAPTION= <scene name='initialview01'>2cep</scene>, resolution 2.2Å | |PDB= 2cep |SIZE=350|CAPTION= <scene name='initialview01'>2cep</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cep OCA], [http://www.ebi.ac.uk/pdbsum/2cep PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cep RCSB]</span> | ||
}} | }} | ||
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[[Category: Kraut, J.]] | [[Category: Kraut, J.]] | ||
[[Category: Miller, M A.]] | [[Category: Miller, M A.]] | ||
| - | [[Category: HEM]] | ||
[[Category: oxidoreductase(h2o2(a))]] | [[Category: oxidoreductase(h2o2(a))]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:20:24 2008'' |
Revision as of 23:20, 30 March 2008
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| , resolution 2.2Å | |||||||
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| Ligands: | |||||||
| Activity: | Cytochrome-c peroxidase, with EC number 1.11.1.5 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ROLE OF MET-230 IN INTRAMOLECULAR ELECTRON TRANSFER BETWEEN THE OXYFERRYL HEME AND TRP 191 IN CYTOCHROME C PEROXIDASE COMPOUND II
Overview
The kinetics of electron transfer from cytochrome c (CC) to yeast cytochrome c peroxidase (CcP) compound I were studied by flash photolysis and stopped-flow spectroscopy. Flash photolysis studies employed horse CC derivatives labeled at specific lysine amino groups with (dicarboxybipyridine)bis-(bipyridine)ruthenium (Ru-CC). Initial electron transfer from Ru-CC reduced the indole radical on Trp-191 of CcP compound I [CMPI(IV,R.)], producing CMPII(IV,R). This reaction was biphasic for each of several Ru-CC derivatives, with rate constants which varied according to the position of the Ru label. For Ru-27-CC labeled at lysine 27, rate constants of 43,000 and 1600 s-1 were observed at pH 5.0 in 2 mM acetate. After reduction of the indole radical by Ru-CC, intramolecular electron transfer from Trp-191 to the oxyferryl heme in CMPII(IV,R) was observed, producing CMPII(III,R.). The rate constant and extent of this intramolecular electron transfer reaction were independent of both the protein concentration and the Ru-CC derivative employed. The rate constant decreased from 1100 s-1 at pH 5 to 550 s-1 at pH 6, while the extent of conversion of CMPII(IV,R) to CMPII(III,R.) decreased from 56% at pH 5 to 29% at pH 6. The reaction was not detected at pH 7.0 and above. The pH dependence of the rate and extent of this internal electron transfer reaction paralleled the pH dependence of the rate of bimolecular reduction of CMPII(IV,R) by native horse CC measured by stopped-flow spectroscopy at high ionic strength.(ABSTRACT TRUNCATED AT 250 WORDS)
About this Structure
2CEP is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II., Liu RQ, Miller MA, Han GW, Hahm S, Geren L, Hibdon S, Kraut J, Durham B, Millett F, Biochemistry. 1994 Jul 26;33(29):8678-85. PMID:8038157
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