Mutagenesis of the conserved lysine 14 of cytochrome c-550 from Thiobacillus versutus affects the protein structure and the electron self-exchange rate

Biochemistry ◽  
1993 ◽  
Vol 32 (50) ◽  
pp. 13893-13901 ◽  
Author(s):  
Marcellus Ubbink ◽  
Gerard W. Canters
Keyword(s):  
Exchange Rate ◽  
Protein Structure ◽  
Cytochrome C ◽  
Thiobacillus Versutus

scholarly journals Studies on the protein structure of cytochrome c by introducing photo-cleavable o-nitrobenzyl derivatives

1999 ◽  
Vol 39 (supplement) ◽  
pp. S160
Author(s):  
S. Hirota ◽  
T. Okuno ◽  
O. Yamauchi
Keyword(s):  
Protein Structure ◽  
Cytochrome C

scholarly journals Properties and Role of Sulphite: Cytochrome c Oxidoreductase Purified from Thiobacillus versutus (A2)

Microbiology ◽  
1984 ◽  
Vol 130 (7) ◽  
pp. 1683-1692 ◽  
Author(s):  
W.-P. LU ◽  
D. P. KELLY
Keyword(s):  
Cytochrome C ◽  
Thiobacillus Versutus

Spectroscopic approach for the interaction of carbon nanoparticles with cytochrome c and BY-2 cells: Protein structure and mitochondrial function

2019 ◽  
Vol 138 ◽  
pp. 29-36 ◽  
Author(s):  
Lijuan Chen ◽  
Jufang Hao ◽  
Liangtao Xu ◽  
Xiangyu Meng ◽  
Xiang Li ◽  
...  
Keyword(s):  
Protein Structure ◽  
Cytochrome C ◽  
Mitochondrial Function ◽  
Carbon Nanoparticles

Gold Nanoparticle−Cytochrome c Complexes:  The Effect of Nanoparticle Ligand Charge on Protein Structure

Langmuir ◽  
2005 ◽  
Vol 21 (26) ◽  
pp. 12080-12084 ◽  
Author(s):  
Marie-Eve Aubin-Tam ◽  
Kimberly Hamad-Schifferli
Keyword(s):  
Protein Structure ◽  
Cytochrome C ◽  
Gold Nanoparticle

scholarly journals The influence of Glu44 and Glu56 of cytochrome b5 on the protein structure and interaction with cytochrome c

1996 ◽  
Vol 9 (7) ◽  
pp. 555-558 ◽  
Author(s):  
Yu-Long Sun ◽  
Yi Xie ◽  
Yun-Hua Wang ◽  
Gu-Tian Xiao ◽  
Zhong-Xian Huang
Keyword(s):  
Protein Structure ◽  
Cytochrome C ◽  
Cytochrome B5

Cobalt, Iron and Ruthenium Complexes of Picolinic and Dipicolinic Acids: Syntheses, Solution Properties and Kinetics of Electron Transfer Reactions With Cytochrome C(II) and Some Inorganic Reductants

1989 ◽  
Vol 42 (1) ◽  
pp. 1 ◽  
Author(s):  
RM Ellis ◽  
JD Quilligan ◽  
NH Williams ◽  
JK Yandell
Keyword(s):  
Exchange Rate ◽  
Cytochrome C ◽  
Rate Constant ◽  
Order Rate Constant ◽  
The Self ◽  
Transfer Reactions ◽  
Solution Properties ◽  
Cobalt Iron ◽  
Exchange Rate Constant ◽  
Kinetics Of

Tris picolinate complexes of CO111 and RU111 have been synthesized, and their standard potentials measured (432 �10, 403 �2 mV) at 25�C and ionic strength 0.1 mol dm-3. The self-exchange rate constant of Ru ( pic )3O/- was found to be (1 .4 �0.9)×108 dm3 mol-1 s-l, from reaction with cytochrome C(II), Co( bpy )32+ and ~Co( phen )32+. For the reaction between Fe( dipic )2- and cytochrome ~(II), at 2S260C, pH 5.5 and I 0.1 mol dm-3 (KNO3), the second-order rate constant was (3.2 �0.l)×105 dm3 mol-1 s-1,with ΔH+ 19.9 �0.9 kJ mol-1 and ΔS+ -72.8 �.7 J K-1 mol-l. The self-exchange rate constant of Fe( dipic )2-/2- was reevaluated as (5.8 �0.2)×106 dm3 mol-l s-1.

scholarly journals Surface Engineering of Gold Nanorods for Cytochrome c Bioconjugation: An Effective Strategy To Preserve the Protein Structure

ACS Omega ◽  
2018 ◽  
Vol 3 (5) ◽  
pp. 4959-4967 ◽  
Author(s):  
Tiziana Placido ◽  
Lorenzo Tognaccini ◽  
Barry D. Howes ◽  
Alessandro Montrone ◽  
Valentino Laquintana ◽  
...  
Keyword(s):  
Protein Structure ◽  
Cytochrome C ◽  
Gold Nanorods ◽  
Surface Engineering ◽  
Effective Strategy

scholarly journals Ionization of tyrosine and lysine residues in native and modified horse cytochrome c

1983 ◽  
Vol 213 (3) ◽  
pp. 679-686 ◽  
Author(s):  
A P Boswell ◽  
G R Moore ◽  
R J P Williams ◽  
D E Harris ◽  
C J A Wallace ◽  
...  
Keyword(s):  
Protein Structure ◽  
Cytochrome C ◽  
Tyrosine Residue ◽  
Alkaline Ph ◽  
Pka Values ◽  
Tyrosine Residues ◽  
Lysine Residues ◽  
Higher Temperature ◽  
Modified Proteins ◽  
Horse Cytochrome

1H-n.m.r. and 13C-n.m.r. spectroscopy of horse cytochrome c and 1H-n.m.r. spectroscopy of the lysine-modified proteins N epsilon-acetimidyl-, N epsilon-amidino-, N epsilon-trifluoroacetyl- and N epsilon-maleyl-cytochrome c have shown that, although the lysine modifications do not greatly perturb the protein structure at pH7 and 27 degrees C, at higher temperature or at alkaline pH some parts of the structure are markedly perturbed. At pH7 and 27 degrees C the region of the protein about Ile-57 is affected in all the modified proteins, though not all to the same degree. N epsilon-Maleylation most seriously affects the protein structure, and the fully maleylated protein is readily unfolded. At 27 degrees C all four of the tyrosine residues of native horse cytochrome c have pKa values above 11, but in N epsilon-acetimidyl-cytochrome c the pKa of one tyrosine residue is 10.2.

Sign in / Sign up

Export Citation Format

Share Document