DC Field | Value | Language |
dc.contributor.author | Goss, Tatjana | |
dc.contributor.author | Hanke, Guy | |
dc.date.accessioned | 2021-12-23T15:56:20Z | - |
dc.date.available | 2021-12-23T15:56:20Z | - |
dc.date.issued | 2014 | |
dc.identifier.issn | 13892037 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/2300 | - |
dc.description.abstract | At the end of the linear photosynthetic electron transfer (PET) chain, the small soluble protein ferredoxin (Fd) transfers electrons to Fd: NADP(H) oxidoreductase (FNR), which can then reduce NADP(+) to support C assimilation. In addition to this linear electron flow (LEF), Fd is also thought to mediate electron flow back to the membrane complexes by different cyclic electron flow (CEF) pathways: either antimycin A sensitive, NAD(P) H complex dependent, or through FNR located at the cytochrome b(6)f complex. Both Fd and FNR are present in higher plant genomes as multiple gene copies, and it is now known that specific Fd iso-proteins can promote CEF. In addition, FNR iso-proteins vary in their ability to dynamically interact with thylakoid membrane complexes, and it has been suggested that this may also play a role in CEF. We will highlight work on the different Fd-isoproteins and FNR-membrane association found in the bundle sheath (BSC) and mesophyll (MC) cell chloroplasts of the C4 plant maize. These two cell types perform predominantly CEF and LEF, and the properties and activities of Fd and FNR in the BSC and MC are therefore specialized for CEF and LEF respectively. A diversity of Fd isoproteins and dynamic FNR location has also been recorded in C3 plants, algae and cyanobacteria. This indicates that the principles learned from the extreme electron transport situations in the BSC and MC of maize might be usefully applied to understanding the dynamic transition between these states in other systems. | |
dc.description.sponsorship | Deutsche Forschungsgemeinschaft SachbeihilfeGerman Research Foundation (DFG) [HA5921/1-1]; COST ActionEuropean Cooperation in Science and Technology (COST) [TD1102]; Funding in the laboratory of G. Hanke and T. Goss from Deutsche Forschungsgemeinschaft Sachbeihilfe HA5921/1-1 is gratefully acknowledged. This publication is supported by Grant of COST Action TD1102. COST (European Cooperation in Science and Technology) is Europe's longest-running intergovernmental framework for cooperation in science and technology funding cooperative scientific projects called `COST Actions'. With a successful history of implementing scientific networking projects for over 40 years, COST offers scientists the opportunity to embark upon bottom-up, multidisciplinary and collaborative networks across all science and technology domains. For more information about COST, please visit www.cost.eu. | |
dc.language.iso | en | |
dc.publisher | BENTHAM SCIENCE PUBL LTD | |
dc.relation.ispartof | CURRENT PROTEIN & PEPTIDE SCIENCE | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | Bundle sheath | |
dc.subject | BUNDLE-SHEATH-CELLS | |
dc.subject | C-4 PHOTOSYNTHESIS | |
dc.subject | CHLOROPHYLL FLUORESCENCE | |
dc.subject | CHLOROPLASTIC NAD(P)H DEHYDROGENASE | |
dc.subject | cyclic electron flow | |
dc.subject | DIFFERENTIAL EXPRESSION | |
dc.subject | ferredoxin | |
dc.subject | FNR | |
dc.subject | mesophyll | |
dc.subject | N-TERMINAL DOMAIN | |
dc.subject | PHOTOSYSTEM-I | |
dc.subject | SPINACH-CHLOROPLASTS | |
dc.subject | THYLAKOID MEMBRANES | |
dc.subject | WATER-WATER CYCLE | |
dc.title | The End of the Line: Can Ferredoxin and Ferredoxin NADP(H) Oxidoreductase Determine the Fate of Photosynthetic Electrons? | |
dc.type | review | |
dc.identifier.doi | 10.2174/1389203715666140327113733 | |
dc.identifier.isi | ISI:000339275200008 | |
dc.description.volume | 15 | |
dc.description.issue | 4 | |
dc.description.startpage | 385 | |
dc.description.endpage | 393 | |
dc.identifier.eissn | 18755550 | |
dc.publisher.place | EXECUTIVE STE Y-2, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATES | |
dcterms.isPartOf.abbreviation | Curr. Protein Pept. Sci. | |
dcterms.oaStatus | Green Submitted, Green Published | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | HaGu059 | - |