2v08
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Cytochrome c6A is a unique dithio-cytochrome of green algae and plants. It | + | Cytochrome c6A is a unique dithio-cytochrome of green algae and plants. It has a very similar core structure to that of bacterial and algal cytochromes c6 but is unable to fulfill the same function of transferring electrons from cytochrome f to photosystem I. A key feature is that its heme midpoint potential is more than 200 mV below that of cytochrome c6 despite having His and Met as axial heme-iron ligands. To identify the molecular origins of the difference in potential, the structure of cytochrome c6 from the cyanobacterium Phormidium laminosum has been determined by X-ray crystallography and compared with the known structure of cytochrome c6A. One salient difference of the heme pockets is that a highly conserved Gln (Q51) in cytochrome c6 is replaced by Val (V52) in c6A. Using protein film voltammetry, we found that swapping these residues raised the c6A potential by +109 mV and decreased that of c6 by almost the same extent, -100 mV. X-ray crystallography of the V52Q protein showed that the Gln residue adopts the same configuration relative to the heme as in cytochrome c6 and we propose that this stereochemistry destabilizes the oxidized form of the heme. Consequently, replacement of Gln by Val was probably a key step in the evolution of cytochrome c6A from cytochrome c6, inhibiting reduction by the cytochrome b6f complex and facilitating establishment of a new function. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Modulation of | + | Modulation of heme redox potential in the cytochrome c6 family., Worrall JA, Schlarb-Ridley BG, Reda T, Marcaida MJ, Moorlen RJ, Wastl J, Hirst J, Bendall DS, Luisi BF, Howe CJ, J Am Chem Soc. 2007 Aug 1;129(30):9468-75. Epub 2007 Jul 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17625855 17625855] |
[[Category: Phormidium laminosum]] | [[Category: Phormidium laminosum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bendall, D | + | [[Category: Bendall, D S.]] |
[[Category: Hirst, J.]] | [[Category: Hirst, J.]] | ||
| - | [[Category: Howe, C | + | [[Category: Howe, C J.]] |
| - | [[Category: Luisi, B | + | [[Category: Luisi, B F.]] |
| - | [[Category: Marcaida, M | + | [[Category: Marcaida, M J.]] |
| - | [[Category: Moorlen, R | + | [[Category: Moorlen, R J.]] |
[[Category: Reda, T.]] | [[Category: Reda, T.]] | ||
| - | [[Category: Schlarb-Ridley, B | + | [[Category: Schlarb-Ridley, B G.]] |
[[Category: Wastl, J.]] | [[Category: Wastl, J.]] | ||
| - | [[Category: Worrall, J | + | [[Category: Worrall, J A.R.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: photosynthesis]] | [[Category: photosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:52:01 2008'' |
Revision as of 16:52, 21 February 2008
|
STRUCTURE OF WILD-TYPE PHORMIDIUM LAMINOSUM CYTOCHROME C6
Overview
Cytochrome c6A is a unique dithio-cytochrome of green algae and plants. It has a very similar core structure to that of bacterial and algal cytochromes c6 but is unable to fulfill the same function of transferring electrons from cytochrome f to photosystem I. A key feature is that its heme midpoint potential is more than 200 mV below that of cytochrome c6 despite having His and Met as axial heme-iron ligands. To identify the molecular origins of the difference in potential, the structure of cytochrome c6 from the cyanobacterium Phormidium laminosum has been determined by X-ray crystallography and compared with the known structure of cytochrome c6A. One salient difference of the heme pockets is that a highly conserved Gln (Q51) in cytochrome c6 is replaced by Val (V52) in c6A. Using protein film voltammetry, we found that swapping these residues raised the c6A potential by +109 mV and decreased that of c6 by almost the same extent, -100 mV. X-ray crystallography of the V52Q protein showed that the Gln residue adopts the same configuration relative to the heme as in cytochrome c6 and we propose that this stereochemistry destabilizes the oxidized form of the heme. Consequently, replacement of Gln by Val was probably a key step in the evolution of cytochrome c6A from cytochrome c6, inhibiting reduction by the cytochrome b6f complex and facilitating establishment of a new function.
About this Structure
2V08 is a Single protein structure of sequence from Phormidium laminosum with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Modulation of heme redox potential in the cytochrome c6 family., Worrall JA, Schlarb-Ridley BG, Reda T, Marcaida MJ, Moorlen RJ, Wastl J, Hirst J, Bendall DS, Luisi BF, Howe CJ, J Am Chem Soc. 2007 Aug 1;129(30):9468-75. Epub 2007 Jul 11. PMID:17625855
Page seeded by OCA on Thu Feb 21 18:52:01 2008
Categories: Phormidium laminosum | Single protein | Bendall, D S. | Hirst, J. | Howe, C J. | Luisi, B F. | Marcaida, M J. | Moorlen, R J. | Reda, T. | Schlarb-Ridley, B G. | Wastl, J. | Worrall, J A.R. | CL | HEM | IMD | ZN | Cyano-bacteria | Cytochrome | Electron-transfer | Photosynthesis
