Related ArticlesCyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2 pH-dependent conformational states.
Eur J Biochem. 1995 Aug 15;232(1):206-13
Authors: Battistuzzi G, Borsari M, Ferretti S, Sola M, Soliani E
The pH-induced protein conformational transitions and changes in the ligation state of the heme iron in cytochrome c2 from Rhodopseudomonas palustris were monitored by electrochemical and spectroscopic measurements. In the pH range 1.5-11, the E degree values (and/or the peak potentials) determined by cyclic voltammetry, the electronic spectra and the hyperfine-shifted 1H-NMR resonances of the protein are sensitive to a number of acid/base equilibria. In particular, four equilibria have been determined for the oxidized protein with pKa values of 2.5, 5.5, 6.6 and 9.0. The lowest pKa most probably involves disruption of both axial heme iron bonds and protein unfolding. The subsequent pKa is associated with a low-pH oxidation of the protein by dioxygen, which is accompanied by a conformational change. The equilibrium with an apparent pKa of 6.6 modulates the E degree values without determining any detectable spectral change and most likely involves the acid/base equilibrium of an histidine residue in close vicinity of the heme (possibly His53). Finally, the alkaline ionization is due to the replacement of the methionine axially bound to the heme iron with a stronger (most probably N-donor) ligand. The reduced alkaline form is unstable and spontaneously converts to the neutral reduced form with a kinetic constant of 0.98 s-1 at pH 9.2.
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...
nmrlearner
Journal club
0
07-26-2011 11:22 PM
[NMR paper] NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c(5
NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c(556).
Related Articles NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c(556).
J Biol Inorg Chem. 2004 Mar;9(2):224-30
Authors: Bertini I, Faraone-Mennella J, Gray HB, Luchinat C, Parigi G, Winkler JR
The structure of oxidized Rhodopseudomonas palustris cytochrome c(556) has been modeled after that of high-spin cytochrome c' from the same bacterium, the latter being the protein with the greatest sequence identity (35%) among...
nmrlearner
Journal club
0
11-24-2010 09:25 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.
Related Articles Interaction of cytochrome c with cytochrome c oxidase: an NMR study on two soluble fragments derived from Paracoccus denitrificans.
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...
nmrlearner
Journal club
0
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.
Related Articles Interaction of yeast iso-1-cytochrome c with cytochrome c peroxidase investigated by heteronuclear NMR spectroscopy.
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...
nmrlearner
Journal club
0
11-19-2010 08:32 PM
[NMR paper] 1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing
1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing a High-Spin Iron(II) Heme Moiety.
Related Articles 1H NMR Study of the Reduced Cytochrome c' from Rhodopseudomonas palustris Containing a High-Spin Iron(II) Heme Moiety.
Inorg Chem. 1998 Sep 21;37(19):4814-4821
Authors: Bertini I, Dikiy A, Luchinat C, Macinai R, Viezzoli MS
The assignment of the hyperfine shifted signals of the reduced cytochrome c' from Rhodopseudomonas palustris has been obtained through saturation transfer experiments with assigned signals...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[NMR paper] Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing su
Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing surface charges through anion-binding studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Cyclic voltammetry and 1H-NMR of Rhodopseudomonas palustris cytochrome c2. Probing surface charges through anion-binding studies.
Eur J Biochem. 1995 Oct 1;233(1):335-9
Authors: Battistuzzi G, Borsari M, Dallari D, Ferretti S, Sola M
The effects of...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependen
1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper.
Related Articles 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper.
Biochemistry. 1991 Oct 1;30(39):9387-95
Authors: Atkinson RA, Saudek V, Huggins JP, Pelton JT
Cyclic GMP dependent protein kinase exists as a dimer in its native form. A peptide corresponding to the dimerization domain in the N-terminal segment has been characterized...
nmrlearner
Journal club
0
08-21-2010 11:12 PM
[NMR paper] 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependen
1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper.
Related Articles 1H NMR and circular dichroism studies of the N-terminal domain of cyclic GMP dependent protein kinase: a leucine/isoleucine zipper.
Biochemistry. 1991 Oct 1;30(39):9387-95
Authors: Atkinson RA, Saudek V, Huggins JP, Pelton JT
Cyclic GMP dependent protein kinase exists as a dimer in its native form. A peptide corresponding to the dimerization domain in the N-terminal segment has been characterized...