| |
Records |
Links |
|
Author |
Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. |
|
| |
Title |
A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) |
Type |
Journal Article |
| |
Year |
1977 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
|
| |
Volume |
77 |
Issue |
1 |
Pages  |
193-199 |
|
| |
Keywords |
Animals; Cyanides; *Cytochrome c Group/metabolism; Ferric Compounds; Horses; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Mathematics; Myocardium/enzymology; *Oligopeptides/metabolism; *Peptide Fragments/metabolism; Protein Binding; Spectrophotometry; Temperature |
|
| |
Abstract |
The ferric form of the haem undecapeptide, derived from horse cytochrome c by peptic digestion, undergoes at least three pH-induced transitions with pK values of 3.4, 5.8 and 7.6. Temperature-jump experiments suggest that the first of these is due to the binding of a deprotonated imidazole group to the feric iron while the second and third arise from the binding of the two available amino groups present (the alpha-NH2 of valine and the epsilon-NH2 of lysine). Molecular models indicate that steric retraints on the peptide dictate that these amino groups may only coordinate to iron atoms via intermolecular bonds, thus leading to the polymerization of the peptide. Cyanide binding studies are in agreement with these conclusions and also yield a value of 3.6 X 10(6) M-1 s-1 for the intrinsic combination constant of CN- anion with the haem. A model is proposed which describes the pH-dependent properties of the ferric undecapeptide. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
English |
Summary Language |
|
Original Title |
|
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
0014-2956 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:20304 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3814 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Wilson, M.T.; Silvestrini, M.C.; Morpurgo, L.; Brunori, M. |
|
| |
Title |
Electron transfer kinetics between Rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and Pseudomonas cytochrome c551) |
Type |
Journal Article |
| |
Year |
1979 |
Publication |
Journal of Inorganic Biochemistry |
Abbreviated Journal |
J Inorg Biochem |
|
| |
Volume |
11 |
Issue |
2 |
Pages |
95-100 |
|
| |
Keywords |
Animals; Copper; Cytochrome c Group/*metabolism; Electron Transport; Kinetics; Metalloproteins/*metabolism; Plant Proteins/*metabolism; *Plants, Toxic; Pseudomonas aeruginosa/*metabolism; Toxicodendron/*metabolism |
|
| |
Abstract |
The electron transfer reactions between Rhus vernicifera stellacyanin and either horse heart cytochrome c or Pseudomonas aeruginosa cytochrome c551 were investigated by rapid reaction techniques. The time course of electron transfer is monophasic under all conditions, and thus consistent with a simple formulation of the reaction. Both stopped-flow and temperature-jump experiments yield equilibrium constants in reasonable agreement with values calculated from the redox potentials. The differences in reaction rate between the two cytochromes and stellacyanin are discussed in terms of the Marcus theory. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
English |
Summary Language |
|
Original Title |
|
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
0162-0134 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:228006 |
Approved |
no |
|
| |
Call Number |
refbase @ user @ |
Serial |
3879 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Kihara, H. |
|
| |
Title |
Comparison of the redox reactions of various types of cytochrome c with iron hexacyanides |
Type |
Journal Article |
| |
Year |
1981 |
Publication |
Biochimica et Biophysica Acta (BBA) – Bioenergetics |
Abbreviated Journal |
|
|
| |
Volume |
634 |
Issue |
|
Pages |
93-104 |
|
| |
Keywords |
Cytochrome c; Redox reaction; Iron hexacyanide; Temperature jump; Electron transfer |
|
| |
Abstract |
The dynamic behavior of various types of cytochromes c in the redox reaction with iron hexacyanides was studied using a temperature-jump method in order to elucidate the molecular mechanism of the redox reaction of cytochromes with their oxidoreductants. Transmittance after the temperature jump changed through a single exponential decay for all cytochromes investigated. Under a constant concentration of anion, the redox reaction of various types of cytochrome c with iron hexacyanides was analyzed according to the scheme: Ki=kt/k-i (i=1,2,3) where C(III) and C(II) are ferric and ferrous cytochromes, respectively, Fe(III) and Fe(II) are ferri- and ferrocyanides, respectively, C(III) [middle dot] Fe(II) is the ferricytochrome-ferrocyanide complex and C(II) [middle dot] Fe(III) is the ferrocytochrome-ferricyanide complex. When step B is slower than the other two steps A and C, τ-1 can be represented approximately as where the bar over the variables denotes the equilibrium value. In a large excess of ferrocyanide against cytochrome, we can estimate k2, k-2, K1 and K3 independently. In the case of horse cytochrome c at 18[degree sign]C in 0.1 M phosphate buffer at pH 7 with 0.3 M KNO3, the estimated parameters are k2 = 100 +/- 50 s-1, k-2 = (3.5 +/- 1.0) [middle dot] 103 s-1, K1 = 15 +/- 7 M-1 and K3 = (8.5 +/- 1.5) [middle dot] 10-4 M. From the same experiments for seven cytochromes (cytochrome c from horse, tuna, Candida krusei, Saccharomyces oviformis, Rhodospirillum rubrum cytochrome c2, Spirulina platensis cytochrome c-554 and Thermus thermophilus cytochrome c-552), the following results can be deduced. (1) Each parameter defined in the scheme above (k2, k-2, K1, K3) diverged beyond the error range. Above all, k2 values of cytochromes c-554 and c-552 are as large as 1 [middle dot] 104 s-1 and much larger than those for the other cytochromes (to 50 approx. 700 S-1). (2) The variance of k2K1 and k-2/K3 are relatively less than the variances of individual parameters (k2, k-2, K1 and K3), which suggests that the values of k2K1 and k-2/K3 have been conserved during the course of evolution. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
|
Summary Language |
|
Original Title |
|
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
|
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
|
Approved |
no |
|
| |
Call Number |
refbase @ user @ |
Serial |
3980 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W. |
|
| |
Title |
Folding units govern the cytochrome c alkaline transition |
Type |
Journal Article |
| |
Year |
2003 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
|
| |
Volume |
331 |
Issue |
1 |
Pages |
37-43 |
|
| |
Keywords |
Animals; Cytochrome c Group/*chemistry; Horses; Hydrogen/chemistry; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; *Protein Folding; Protein Structure, Tertiary; Spectrum Analysis; Titrimetry |
|
| |
Abstract |
The alkaline transition of cytochrome c is a model for protein structural switching in which the normal heme ligand is replaced by another group. Stopped flow data following a jump to high pH detect two slow kinetic phases, suggesting two rate-limiting structure changes. Results described here indicate that these events are controlled by the same structural unfolding reactions that account for the first two steps in the reversible unfolding pathway of cytochrome c. These and other results show that the cooperative folding-unfolding behavior of protein foldons can account for a variety of functional activities in addition to determining folding pathways. |
|
| |
Address |
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.upenn.edu |
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
English |
Summary Language |
|
Original Title |
|
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
0022-2836 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:12875834 |
Approved |
no |
|
| |
Call Number |
Equine Behaviour @ team @ |
Serial |
3781 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Saigo, S. |
|
| |
Title |
Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c |
Type |
Journal Article |
| |
Year |
1981 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
|
| |
Volume |
669 |
Issue |
1 |
Pages |
13-20 |
|
| |
Keywords |
Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism |
|
| |
Abstract |
Equilibria and kinetics of alkaline isomerization of seven ferricytochromes c from vertebrates were studied by pH-titration and pH-jump methods in the pH region of 7-12. In the equilibrium behavior, no significant difference was detected among the cytochromes c, whereas marked differences in the kinetic behavior were observed. According to the kinetic behavior of the isomerization, the cytochromes c examined fall into three classes: Group I (horse, sheep, dog and pigeon cytochromes c), Group II (tuna and bonito cytochromes c) and Group III (rhesus monkey cytochrome c). The kinetic results are interpreted in terms of the sequential scheme: Neutral form in equilibrium with fast Transient form in equilibrium with slow Alkaline form where the neutral and alkaline forms are the species stable at neutral and alkaline pH, respectively, and the transient form is a kinetic intermediate. From comparison of the primary sequences of the seven cytochromes c and the classification of these cytochromes c, it is concluded that the amino acid substitution Phe/Tyr at the 46-th position has a major influence on the kinetic behavior. In Group II and III cytochromes c, the ionization of Tyr-46 is suggested to bring about loosening of the heme crevice and thus facilitate the ligand replacement involved in the isomerization. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
English |
Summary Language |
|
Original Title |
|
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
0006-3002 |
ISBN |
|
Medium |
|
|
| |
Area |
|
Expedition |
|
Conference |
|
|
| |
Notes |
PMID:6271238 |
Approved |
no |
|
| |
Call Number |
refbase @ user @ |
Serial |
3871 |
|
| Permanent link to this record |
