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Mostrando ítems 1-10 de 21
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
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 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
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 ...
Artículo
NMR analysis of the transient complex between membrane photosystem I and soluble cytochrome c6
(Elsevier, 2005)
A structural analysis of the surface areas of cytochrome c6, responsible for the transient interaction with photosystem I, was performed by NMR transverse relaxation-optimized spectroscopy. The hemeprotein was titrated by ...
Artículo
Structural and Functional Analysis of Novel Human Cytochrome c Targets in Apoptosis
(American Society for Biochemistry and Molecular Biology, 2014)
Since the first description of apoptosis four decades ago, great efforts have been made to elucidate, both in vivo and in vitro, the molecular mechanisms involved in its regulation. Although the role of cytochrome c during ...
Artículo
Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c
(National Academy of Sciences, 2015)
Chromatin is pivotal for regulation of the DNA damage process insofar as it influences access to DNA and serves as a DNA repair docking site. Recent works identify histone chaperones as key regulators of damaged chromatin’s ...