| dc.creator |
Bernal Ibáñez, María |
|
| dc.creator |
Roncel Gil, Mercedes |
|
| dc.creator |
Ortega, José M. |
|
| dc.creator |
Picorel Castaño, Rafael |
|
| dc.creator |
Yruela Guerrero, Inmaculada |
|
| dc.date |
2008-04-15T09:01:32Z |
|
| dc.date |
2008-04-15T09:01:32Z |
|
| dc.date |
2004-04 |
|
| dc.date.accessioned |
2017-01-31T01:02:18Z |
|
| dc.date.available |
2017-01-31T01:02:18Z |
|
| dc.identifier |
Physiologia Plantarum 120 (4) , 686–694 |
|
| dc.identifier |
0031-9317 |
|
| dc.identifier |
http://hdl.handle.net/10261/3580 |
|
| dc.identifier |
10.1111/j.1399-3054.2004.0286.x |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3580 |
|
| dc.description |
The definitive version is available at www.blackwell-synergy.com |
|
| dc.description |
Toxic Cu(II) effect on Cytochrome b559 under aerobic photoinhibitory conditions was examined in two different PSII membrane preparations active in oxygen evolution. The preparations differ in the content of Cytochrome b559 redox potential forms. Difference absorption spectra showed that the presence of Cu(II) induced the oxidation of the high-potential form of Cytochrome b559 in the dark. Addition of hydroquinone reduced the total oxidised high-potential form of Cytochrome b559 present in Cu(II)-treated PSII membranes indicating that no conversion to the low-potential form took place. Spectroscopic determinations of Cytochrome b559 during photoinhibitory treatment showed slower kinetics of Cu(II) effect on Cytochrome b559 as compared to the rapid loss of oxygen evolution activity in the same conditions. This result indicates that Cytochrome b559 is affected after PSII centers are photoinhibited. The high-potential form was more sensitive to toxic Cu(II) action than the low-potential form under illumination at pH 6.0. The content of the high-potential form of Cytochrome b559 was completely lost, however the low-potential content was unaffected in these conditions. This loss did not involve cytochrome protein degradation. Results are discussed in terms of different binding properties of the heme iron to the protonated or unprotonated histidine ligand in the high-potential and low-potential forms of Cytochrome b559, respectively. |
|
| dc.description |
M. Bernal was recipient of an I3P Programme fellowship from Consejo Superior de Investigaciones Científicas. This work was supported by the Dirección General de Investigación (Grant BMC2002-00031) to R.P. and Gobierno de Aragón (Grant P015/2001) to I.Y., and it has been done within GC DGA 2002 Program of Gobierno de Aragón. |
|
| dc.description |
Peer reviewed |
|
| dc.format |
263483 bytes |
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| dc.format |
application/pdf |
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| dc.language |
eng |
|
| dc.publisher |
Blackwell Publishing |
|
| dc.rights |
openAccess |
|
| dc.subject |
cytochrome b559 |
|
| dc.subject |
copper |
|
| dc.subject |
photosystem II |
|
| dc.subject |
photoinhibition |
|
| dc.subject |
redox potential |
|
| dc.title |
Copper effect on cytochrome b559 of photosystem II under photoinhibitory conditions |
|
| dc.type |
Artículo |
|