1i54: Difference between revisions
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|PDB= 1i54 |SIZE=350|CAPTION= <scene name='initialview01'>1i54</scene>, resolution 1.50Å | |PDB= 1i54 |SIZE=350|CAPTION= <scene name='initialview01'>1i54</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZNH:PROTOPORPHYRIN+IX+CONTAINING+ZN'>ZNH</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[3cyt|3CYT]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i54 OCA], [http://www.ebi.ac.uk/pdbsum/1i54 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i54 RCSB]</span> | |||
}} | }} | ||
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[[Category: Tezcan, F A.]] | [[Category: Tezcan, F A.]] | ||
[[Category: Winkler, J R.]] | [[Category: Winkler, J R.]] | ||
[[Category: cytochrome c]] | [[Category: cytochrome c]] | ||
[[Category: mixed-metal]] | [[Category: mixed-metal]] | ||
[[Category: zinc-porphyrin]] | [[Category: zinc-porphyrin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:46 2008'' | ||
Revision as of 21:14, 30 March 2008
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| , resolution 1.50Å | |||||||
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| Ligands: | , | ||||||
| Related: | 3CYT
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CYTOCHROME C (TUNA) 2FE:1ZN MIXED-METAL PORPHYRINS
OverviewOverview
The current understanding of electron tunneling through proteins has come from work on systems where donors and acceptors are held at fixed distances and orientations. The factors that control electron flow between proteins are less well understood, owing to uncertainties in the relative orientations and structures of the reactants during the very short time that tunneling occurs. As we report here, the way around such structural ambiguity is to examine oxidation-reduction reactions in protein crystals. Accordingly, we have measured and analyzed the kinetics of electron transfer between native and Zn-substituted tuna cytochrome c (cyt c) molecules in crystals of known structure. Electron transfer rates [(320 s(-1) for *Zn-cyt c --> Fe(III)-cyt c; 2000 s(-1) for Fe(II)-cyt c --> Zn-cyt c(+))] over a Zn-Fe distance of 24.1 A closely match those for intraprotein electron tunneling over similar donor-acceptor separations. Our results indicate that van der Waals interactions and water-mediated hydrogen bonds are effective coupling elements for tunneling across a protein-protein interface.
About this StructureAbout this Structure
1I54 is a Single protein structure of sequence from Thunnus thynnus. Full crystallographic information is available from OCA.
ReferenceReference
Electron tunneling in protein crystals., Tezcan FA, Crane BR, Winkler JR, Gray HB, Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):5002-6. Epub 2001 Apr 10. PMID:11296248
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