Guanidine hydrochloride-induced equilibrium unfolding of mutant forms of iso-1-cytochrome c with replacement of proline-71

Biochemistry ◽  
1986 ◽  
Vol 25 (22) ◽  
pp. 6952-6958 ◽  
Author(s):  
Latha Ramdas ◽  
Fred Sherman ◽  
Barry T. Nall
Keyword(s):  
Cytochrome C ◽  
Guanidine Hydrochloride ◽  
Equilibrium Unfolding ◽  
Mutant Forms

Importance of Lysine 79 in Apoptosis Induced by Mutant Forms of Cytochrome C

2012 ◽  
Vol 53 ◽  
pp. S47-S48
Author(s):  
Katia Cristina Ugolini Mugnol ◽  
Débora Martins de Andrade Caselli ◽  
Ingrid Mito de Paula ◽  
Aline de Barros Tirelli ◽  
Verónica Tórtora ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Mutant Forms

scholarly journals Investigations of the Low-Frequency Spectral Density of Cytochrome c upon Equilibrium Unfolding

2013 ◽  
Vol 117 (33) ◽  
pp. 9615-9625 ◽  
Author(s):  
Yuhan Sun ◽  
Venugopal Karunakaran ◽  
Paul M. Champion
Keyword(s):  
Cytochrome C ◽  
Spectral Density ◽  
Low Frequency ◽  
Equilibrium Unfolding

Construction of histidine-tagged yeast mitochondrial cytochrome c oxidase for facile purification of mutant forms

2012 ◽  
Vol 444 (2) ◽  
pp. 199-204 ◽  
Author(s):  
Brigitte Meunier ◽  
Amandine Maréchal ◽  
Peter R. Rich
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Point Mutations ◽  
Normal Functioning ◽  
Yeast Saccharomyces Cerevisiae ◽  
C Terminus ◽  
Radical State ◽  
Uv Visible ◽  
H Channels ◽  
Mutant Forms

Yeast CcO (cytochrome c oxidase) has been developed as a facile system for the production and analysis of mutants of a mitochondrial form of CcO for mechanistic studies. First, a 6H tag (His6 tag) was fused to the C-terminus of a nuclear-encoded subunit of CcO from yeast Saccharomyces cerevisiae. This allowed efficient purification of a WT (wild-type) mitochondrial CcO, 6H-WT (yeast CcO with a 6H tag on the nuclear-encoded Cox13 subunit), with a recovery yield of 45%. Its catalytic-centre activity [≈180 e·s−1 (electrons per s)], UV–visible signatures of oxidized and reduced states and ability to form the PM [‘peroxy’ (but actually a ferryl/radical state)] and F (ferryl) intermediates confirm normal functioning of the histidine-tagged protein. Point mutations were introduced into subunit I of the 6H-WT strain. All mutants were screened for their ability to assemble CcO and grow on respiratory substrate. One such mutant [6H-E243DI (the 6H-WT strain with an additional mutation of E243D in mitochondrial DNA-encoded subunit I)] was purified and showed ~50% of the 6H-WT catalytic-centre activity, consistent with the effects of the equivalent mutation in bacterial oxidases. Mutations in both the D and the H channels affect respiratory growth and these effects are discussed in terms of their putative roles in CcO mechanism.

Characterization of the guanidine-hydrochloride-denatured state of iso-1-cytochrome c by infrared spectroscopy

Biochemistry ◽  
1994 ◽  
Vol 33 (9) ◽  
pp. 2402-2408 ◽  
Author(s):  
Bruce E. Bowler ◽  
Aichun Dong ◽  
Winslow S. Caughey
Keyword(s):  
Infrared Spectroscopy ◽  
Cytochrome C ◽  
Guanidine Hydrochloride ◽  
Denatured State

Equilibrium unfolding of DLC8 monomer by urea and guanidine hydrochloride: Distinctive global and residue level features

Biochimie ◽  
2007 ◽  
Vol 89 (1) ◽  
pp. 117-134 ◽  
Author(s):  
Amarnath Chatterjee ◽  
P.M. Krishna Mohan ◽  
Arati Prabhu ◽  
Anindya Ghosh-Roy ◽  
Ramakrishna V. Hosur
Keyword(s):  
Guanidine Hydrochloride ◽  
Residue Level ◽  
Equilibrium Unfolding
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