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Mostrando ítems 1-10 de 26
Artículo
Site-directed Mutagenesis of Cytochromec 6 from Synechocystissp. PCC 6803
(Elsevier, 1999)
This paper reports the first site-directed mutagenesis analysis of any cytochrome c 6, a heme protein that performs the same function as the copper-protein plastocyanin in the electron transport chain of photosynthetic ...
Artículo
Communication between L–galactono–1,4–lactone dehydrogenase and cytochrome c
(Wiley: FEBS Journal, 2013-02-25)
l‐galactono‐1,4‐lactone dehydrogenase (GALDH) catalyzes the terminal step of vitamin C biosynthesis in plant mitochondria. Here we investigated the communication between Arabidopsis thaliana GALDH and its natural electron ...
Artículo
The dynamic complex of cytochrome c6 and cytochrome f studied with paramagnetic NMR spectroscopy
(Elsevier B.V., 2014)
The rapid transfer of electrons in the photosynthetic redox chain is achieved by the formation of short-lived complexes of cytochrome b6f with the electron transfer proteins plastocyanin and cytochrome c6. A balance must ...
Artículo
Cytochrome c signalosome in mitochondria
(Springer, 2011)
Cytochrome c delicately tilts the balance between cell life (respiration) and cell death (apoptosis). Whereas cell life is governed by transient electron transfer interactions of cytochrome c inside the mitochondria, the ...
Artículo
The Efficient Functioning of Photosynthesis and Respiration in Synechocystis sp. PCC 6803 Strictly Requires the Presence of either Cytochrome c6 or Plastocyanin
(Elsevier, 2004)
In cyanobacteria, cytochrome c6 and plastocyanin are able to replace each other as redox carriers in the photosynthetic and respiratory electron transport chains with the synthesis of one or another protein being regulated ...
Artículo
The cytochrome f–plastocyanin complex as a model to study transient interactions between redox proteins
(Wiley, 2012)
Transient complexes, with a lifetime ranging between microseconds and seconds, are essential forbiochemical reactions requiring a fast turnover. That is the case of the interactions between proteinsengaged in electron ...
Artículo
Cytochrome c1 exhibits two binding sites for cytochrome c in plants
(Elsevier, 2014)
n plants, channeling of cytochrome c molecules between complexes III and IV has been purported to shuttle electrons within the supercomplexes instead of carrying electrons by random diffusion across the intermembrane bulk ...
Artículo
Structure of the Complex between Plastocyanin and Cytochrome f from the Cyanobacterium Nostoc sp. PCC 7119 as Determined by Paramagnetic NMR
(Elsevier, 2005)
The complex between cytochrome f and plastocyanin from the cyanobacterium Nostoc has been characterized by NMR spectroscopy. The binding constant is 16 mm–1, and the lifetime of the complex is much less than 10 ms. ...
Artículo
A Single Arginyl Residue in Plastocyanin and in Cytochrome c6 from the Cyanobacterium Anabaenasp. PCC 7119 Is Required for Efficient Reduction of Photosystem I
(Elsevier, 2001)
Positively charged plastocyanin from Anabaena sp. PCC 7119 was investigated by site-directed mutagenesis. The reactivity of its mutants toward photosystem I was analyzed by laser flash spectroscopy. Replacement of arginine ...
Artículo
Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength
(Elsevier, 2015)
The transient interactions of respiratory cytochrome c with complexes III and IV is herein investigated by using heterologous proteins, namely human cytochrome c, the soluble domain of plant cytochrome c1 and bovine ...