CONCLUSIONS: Together with functional analysis of purified CytcO, we suggest that this ATP interaction is inhibitory of catalytic activity. Our results shed light on the structural flexibility of an important subunit of yeast CytcO and provide structure-based insight into how ATP could regulate mitochondrial respiration.
Using Tryptophan Mutants To Probe the Structural andFunctional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis
Using Tryptophan Mutants To Probe the Structural andFunctional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00833/20171117/images/medium/bi-2017-00833p_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00833
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11-20-2017 02:16 PM
[NMR paper] Solution NMR structure of GATase subunit and structural basis of interaction between GATase and ATPPase subunits in a two-subunit-type GMPS from Methanocaldococcus jannaschii.
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Biochemistry. 2013 May 31;
Authors: Ali R, Kumar S, Balaram H, Sarma SP
Abstract
The solution structure of the monomeric glutamine amidotransferase (GATase) subunit of the...
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06-04-2013 06:31 PM
[NMR paper] Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
J Biomol NMR. 2013 May 25;
Authors: Volkov AN, van Nuland NA
Abstract
Here we present a solution NMR study of the complex between yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP), a paradigm for understanding the biological electron transfer. Performed for the first time, the CcP-observed heteronuclear NMR experiments were used to probe the Cc binding in solution....
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05-28-2013 06:36 PM
NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase [Biochemistry]
NMR basis for interprotein electron transfer gating between cytochrome c and cytochrome c oxidase
Sakamoto, K., Kamiya, M., Imai, M., Shinzawa-Itoh, K., Uchida, T., Kawano, K., Yoshikawa, S., Ishimori, K....
Date: 2011-07-26
The final interprotein electron transfer (ET) in the mammalian respiratory chain, from cytochrome c (Cyt c) to cytochrome c oxidase (CcO) is investigated by 1H-15N heteronuclear single quantum coherence spectral analysis. The chemical shift perturbation in isotope-labeled Cyt c induced by addition of unlabeled CcO indicates that the hydrophobic heme periphery and...
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07-26-2011 11:22 PM
[NMR paper] Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fr
Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
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Biochemistry. 2003 May 27;42(20):6005-12
Authors: Wienk H, Maneg O, Lücke C, Pristovsek P, Löhr F, Ludwig B, Rüterjans H
The functional interactions between the various components of the respiratory chain are relatively short-lived, thus allowing high turnover numbers...
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11-24-2010 09:01 PM
[NMR paper] Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by
Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy.
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Biochemistry. 2001 Jun 19;40(24):7069-76
Authors: Worrall JA, Kolczak U, Canters GW, Ubbink M
The interaction of yeast iso-1-cytochrome c with its physiological redox partner cytochrome c peroxidase has been investigated using heteronuclear NMR techniques. Chemical shift perturbations for both...
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[NMR paper] NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c i
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
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Eur J Biochem. 1991 Dec 5;202(2):339-47
Authors: Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M,...
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08-21-2010 11:12 PM
[NMR paper] NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c i
NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted.
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Eur J Biochem. 1991 Dec 5;202(2):339-47
Authors: Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M,...
NMR structural analysis of the yeast cytochrome c oxidase subunit Cox13 and its interaction with ATP
Linear Mode
