Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00427/20160525/images/medium/bi-2016-00427z_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00427
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/rjyqRfBOAi4
More...
nmrlearner
Journal club
0
05-27-2016 04:11 AM
Cytoplasmic Heme-Binding Protein (HutX) from Vibrio cholerae Is an Intracellular Heme Transport Proteinfor the Heme-Degrading Enzyme, HutZ
Cytoplasmic Heme-Binding Protein (HutX) from Vibrio cholerae Is an Intracellular Heme Transport Proteinfor the Heme-Degrading Enzyme, HutZ
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01273/20160203/images/medium/bi-2015-01273d_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01273
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/TZY3CBAo0xw
More...
nmrlearner
Journal club
0
02-04-2016 11:46 AM
[NMR paper] Proton NMR study of the heme environment in bacterial quinol oxidases.
Proton NMR study of the heme environment in bacterial quinol oxidases.
Related Articles Proton NMR study of the heme environment in bacterial quinol oxidases.
Arch Biochem Biophys. 2004 Jan 15;421(2):186-91
Authors: Zhang J, Osborne JP, Gennis RB, Wang X
The heme environment and ligand binding properties of two relatively large membrane proteins containing multiple paramagnetic metal centers, cytochrome bo3 and bd quinol oxidases, have been studied by high field proton nuclear magnetic resonance (NMR) spectroscopy. The oxidized bo3 enzyme...
nmrlearner
Journal club
0
11-24-2010 09:25 PM
[NMR paper] Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C
Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Related Articles Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Biochemistry. 1994 May 31;33(21):6433-41
Authors: Pochapsky TC, Ratnaswamy G, Patera A
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) and...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C
Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Related Articles Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Biochemistry. 1994 May 31;33(21):6433-41
Authors: Pochapsky TC, Ratnaswamy G, Patera A
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) and...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conf
1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
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 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
Eur J Biochem. 1993 Feb 1;211(3):555-62
Authors: Turner DL, Williams RJ
The redox-state dependent changes in chemical shift, which have...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F b
Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F by 1H-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F by 1H-NMR.
FEBS Lett. 1991 Jul 8;285(1):149-51
Authors: Park JS, Kano K, Niki K, Akutsu H
Site-specific heme assignment of the 1H-NMR spectrum of cytochrome c3 of D. vulgaris Miyazaki F, a tetraheme protein, was established. The major reduction...
nmrlearner
Journal club
0
08-21-2010 11:12 PM
[NMR paper] Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F b
Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F by 1H-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F by 1H-NMR.
FEBS Lett. 1991 Jul 8;285(1):149-51
Authors: Park JS, Kano K, Niki K, Akutsu H
Site-specific heme assignment of the 1H-NMR spectrum of cytochrome c3 of D. vulgaris Miyazaki F, a tetraheme protein, was established. The major reduction...
Redox-Dependent Dynamics in Heme-Bound Bacterial IronResponse Regulator (Irr) Protein
Linear Mode
