dc.identifier.uri |
http://dx.doi.org/10.15488/11655 |
|
dc.identifier.uri |
https://www.repo.uni-hannover.de/handle/123456789/11748 |
|
dc.contributor.author |
Fromm, Steffanie
|
eng |
dc.contributor.author |
Senkler, Jennifer
|
eng |
dc.contributor.author |
Zabaleta, Eduardo
|
eng |
dc.contributor.author |
Peterhänsel, Christoph
|
eng |
dc.contributor.author |
Braun, Hans-Peter
|
eng |
dc.date.accessioned |
2022-01-11T13:13:32Z |
|
dc.date.available |
2022-01-11T13:13:32Z |
|
dc.date.issued |
2016 |
eng |
dc.identifier.citation |
Fromm, S.; Senkler, J.; Zabaleta, E.; Peterhänsel, C.; Braun, H.-P.: The carbonic anhydrase domain of plant mitochondrial complex I. In: Physiologia Plantarum 157 (2016), Nr. 3, S. 289-296. DOI: https://doi.org/10.1111/ppl.12424 |
eng |
dc.description.abstract |
The mitochondrial NADH dehydrogenase complex (complex I) consists of several functional domains which independently arose during evolution. In higher plants, it contains an additional domain which includes proteins resembling gamma-type carbonic anhydrases. The Arabidopsis genome codes for five complex I-integrated gamma-type carbonic anhydrases (γCA1, γCA2, γCA3, γCAL1, γCAL2), but only three copies of this group of proteins form an individual extra domain. Biochemical analyses revealed that the domain is composed of one copy of either γCAL1 or γCAL2 plus two copies of the γCA1/γCA2 proteins. Thus, the carbonic anhydrase domain can have six distinct subunit configurations. Single and double mutants with respect to the γCA/γCAL proteins were employed to genetically dissect the function of the domain. New insights into complex I biology in plants will be reviewed and discussed. © 2016 Scandinavian Plant Physiology Society. |
eng |
dc.language.iso |
eng |
eng |
dc.publisher |
Oxford [u.a.] : Wiley-Blackwell |
eng |
dc.relation.ispartofseries |
Physiologia Plantarum 157 (2016), Nr. 3 |
eng |
dc.rights |
Es gilt deutsches Urheberrecht. Das Dokument darf zum eigenen Gebrauch kostenfrei genutzt, aber nicht im Internet bereitgestellt oder an Außenstehende weitergegeben werden. |
eng |
dc.subject |
Arabidopsis protein |
eng |
dc.subject |
carbonate dehydratase |
eng |
dc.subject |
mitochondrial protein |
eng |
dc.subject |
reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone) |
eng |
dc.subject |
Arabidopsis |
eng |
dc.subject |
chemistry |
eng |
dc.subject |
enzymology |
eng |
dc.subject |
genetics |
eng |
dc.subject |
metabolism |
eng |
dc.subject |
mitochondrion |
eng |
dc.subject |
mutation |
eng |
dc.subject |
Arabidopsis |
eng |
dc.subject |
Arabidopsis Proteins |
eng |
dc.subject |
Carbonic Anhydrases |
eng |
dc.subject |
Electron Transport Complex I |
eng |
dc.subject |
Mitochondria |
eng |
dc.subject |
Mitochondrial Proteins |
eng |
dc.subject |
Mutation |
eng |
dc.subject.ddc |
580 | Pflanzen (Botanik)
|
|
dc.title |
The carbonic anhydrase domain of plant mitochondrial complex I |
eng |
dc.type |
Article |
eng |
dc.type |
Text |
eng |
dc.relation.essn |
1399-3054 |
eng |
dc.relation.issn |
0031-9317 |
eng |
dc.relation.doi |
https://doi.org/10.1111/ppl.12424 |
eng |
dc.bibliographicCitation.issue |
3 |
|
dc.bibliographicCitation.volume |
157 |
|
dc.bibliographicCitation.firstPage |
289 |
|
dc.bibliographicCitation.lastPage |
296 |
|
dc.description.version |
acceptedVersion |
eng |
tib.accessRights |
frei zug�nglich |
eng |