scholarly journals Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation

2020 ◽  
Vol 21 (6) ◽  
pp. 2134
Author(s):  
Daniela Lalli ◽  
Camilla Rosa ◽  
Marco Allegrozzi ◽  
Paola Turano

It is well known that axial coordination of heme iron in mitochondrial cytochrome c has redox-dependent stability. The Met80 heme iron axial ligand in the ferric form of the protein is relatively labile and can be easily replaced by alternative amino acid side chains under non-native conditions induced by alkaline pH, high temperature, or denaturing agents. Here, we showed a redox-dependent destabilization induced in human cytochrome c by substituting Phe82—conserved amino acid and a key actor in cytochrome c intermolecular interactions—with a Lys residue. Introducing a positive charge at position 82 did not significantly affect the structure of ferrous cytochrome c but caused localized unfolding of the distal site in the ferric state. As revealed by 1H NMR fingerprint, the ferric form of the F82K variant had axial coordination resembling the renowned alkaline species, where the detachment of the native Met80 ligand favored the formation of multiple conformations involving distal Lys residues binding to iron, but with more limited overall structural destabilization.

1988 ◽  
Vol 104 (3) ◽  
pp. 477-480 ◽  
Author(s):  
Yoshikazu Tanaka ◽  
Toshihiko Ashikari ◽  
Yuji Shibano ◽  
Teruo Amachi ◽  
Hajime Yoshizumi ◽  
...  

1991 ◽  
Vol 274 (3) ◽  
pp. 825-831 ◽  
Author(s):  
R P Ambler ◽  
M Daniel

The amino acid sequence of rattlesnake cytochrome c was originally reported in 1965, and was one of the earlier sequences to be studied. When compared with other mitochondrial cytochromes c, the snake sequence was soon seen to be anomalous. There were several positions in which the snake protein resembled human cytochrome c, although comparable anomalies were not reported for the protein from other reptiles such as lizard and turtle. Explanations of these results have included accelerated evolution in the snake lineage, paralogy rather than orthology, and faulty determination of the sequence, and the rattlesnake is now often omitted from cytochrome c phylogenetic trees. We have re-investigated the sequence of the snake protein, and believe that the correct sequence differs in nine places from that used for evolutionary theorizing since 1965. Four of these differences are near the haem-attachment site, in a region that was only analysed for amino acid composition in the original investigation. The other five differences are towards the C-terminus of the molecule, and can be explained as being due to the wrong ordering of amino acids within peptides that had been satisfactorily purified. Despite these corrections, the rattlesnake cytochrome c sequence still more closely resembles human cytochrome c than it does that of any other protein we know. We believe that this is an example of convergent evolution, although it does appear that there has been accelerated change in the line connecting the rattlesnake to the ancestral vertebrate line. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50162 (16 pages) at the British Library Document Supply Centre, Boston Spa. Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1991) 273, 5.


2003 ◽  
Vol 312 (3) ◽  
pp. 733-740 ◽  
Author(s):  
Alina Olteanu ◽  
Chetan N Patel ◽  
Matthew M Dedmon ◽  
Scott Kennedy ◽  
Michael W Linhoff ◽  
...  

1991 ◽  
Vol 173 (6) ◽  
pp. 1433-1439 ◽  
Author(s):  
R H Lin ◽  
M J Mamula ◽  
J A Hardin ◽  
C A Janeway

A novel mechanism for breaking T cell self tolerance is described. B cells induced to make autoantibody by immunization of mice with the non-self protein human cytochrome c can present the self protein mouse cytochrome c to autoreactive T cells in immunogenic form. This mechanism of breaking T cell self tolerance could account for the role of foreign antigens in breaking not only B cell but also T cell self tolerance, leading to sustained autoantibody production in the absence of the foreign antigen.


2013 ◽  
Vol 18 (3) ◽  
pp. 289-297 ◽  
Author(s):  
Tracy M. Josephs ◽  
Matthew D. Liptak ◽  
Gillian Hughes ◽  
Alexandra Lo ◽  
Rebecca M. Smith ◽  
...  

Biochemistry ◽  
2018 ◽  
Vol 57 (29) ◽  
pp. 4276-4288 ◽  
Author(s):  
Oliver M. Deacon ◽  
Dimitri A. Svistunenko ◽  
Geoffrey R. Moore ◽  
Michael T. Wilson ◽  
Jonathan A.R. Worrall

Gene ◽  
1991 ◽  
Vol 102 (2) ◽  
pp. 229-236 ◽  
Author(s):  
Roque D. Carrero-Valenzuela ◽  
Franklin Quan ◽  
Robert Lightowlers ◽  
Nancy G. Kennaway ◽  
Michael Litt ◽  
...  

2007 ◽  
Vol 5 (1) ◽  
pp. 9-20 ◽  
Author(s):  
Scot C. Leary ◽  
Paul A. Cobine ◽  
Brett A. Kaufman ◽  
Guy-Hellen Guercin ◽  
Andre Mattman ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document