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Author  |
Pierce, M.M.; Nall, B.T. |
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Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
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Journal Article |
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Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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Volume |
298 |
Issue |
5 |
Pages |
955-969 |
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Keywords |
Amino Acid Sequence; Amino Acid Substitution/genetics; Binding Sites; Cytochrome c Group/*chemistry/genetics/*metabolism; *Cytochromes c; Enzyme Stability/drug effects; Fluorescence; Guanidine/pharmacology; Heme/*metabolism; Histidine/genetics/*metabolism; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation/genetics; Proline/*chemistry/metabolism; Protein Conformation/drug effects; Protein Denaturation/drug effects; *Protein Folding; Protein Renaturation; Saccharomyces cerevisiae/enzymology/genetics; Sequence Alignment; Thermodynamics |
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The effect of His-heme misligation on folding has been investigated for a triple mutant of yeast iso-2 cytochrome c (N26H,H33N,H39K iso-2). The variant contains a single misligating His residue at position 26, a location at which His residues are found in several cytochrome c homologues, including horse, tuna, and yeast iso-1. The amplitude for fast phase folding exhibits a strong initial pH dependence. For GdnHCl unfolded protein at an initial pH<5, the observed refolding at final pH 6 is dominated by a fast phase (tau(2f)=20 ms, alpha(2f)=90 %) that represents folding in the absence of misligation. For unfolded protein at initial pH 6, folding at final pH 6 occurs in a fast phase of reduced amplitude (alpha(2f) approximately 20 %) but the same rate (tau(2f)=20 ms), and in two slower phases (tau(m)=6-8 seconds, alpha(m) approximately 45 %; and tau(1b)=16-20 seconds, alpha(1b) approximately 35 %). Double jump experiments show that the initial pH dependence of the folding amplitudes results from a slow pH-dependent equilibrium between fast and slow folding species present in the unfolded protein. The slow equilibrium arises from coupling of the His protonation equilibrium to His-heme misligation and proline isomerization. Specifically, Pro25 is predominantly in trans in the unligated low-pH unfolded protein, but is constrained in a non-native cis isomerization state by His26-heme misligation near neutral pH. Refolding from the misligated unfolded form proceeds slowly due to the large energetic barrier required for proline isomerization and displacement of the misligated His26-heme ligand. |
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Center for Biomolecular Structure, Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA |
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0022-2836 |
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PMID:10801361 |
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Call Number |
refbase @ user @ |
Serial |
3853 |
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Author |
Ridge, J.A.; Baldwin, R.L.; Labhardt, A.M. |
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Title |
Nature of the fast and slow refolding reactions of iron(III) cytochrome c |
Type |
Journal Article |
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Year |
1981 |
Publication |
Biochemistry |
Abbreviated Journal |
Biochemistry |
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Volume |
20 |
Issue |
6 |
Pages |
1622-1630 |
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Keywords |
Animals; Ascorbic Acid; *Cytochrome c Group; Guanidines; Horses; Kinetics; Oxidation-Reduction; Protein Conformation; Spectrum Analysis |
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Abstract |
The fast and slow refolding reactions of iron(III) cytochrome c (Fe(III) cyt c), previously studied by Ikai et al. (Ikai, A., Fish, W. W., & Tanford, C. (1973) J. Mol. Biol. 73, 165--184), have been reinvestigated. The fast reaction has the major amplitude (78%) and is 100-fold faster than the slow reaction in these conditions (pH 7.2, 25 degrees C, 1.75 M guanidine hydrochloride). We show here that native cyt c is the product formed in the fast reaction as well as in the slow reaction. Two probes have been used to test for formation of native cyt c. absorbance in the 695-nm band and rate of reduction of by L-ascorbate. Different unfolded species (UF, US) give rise to the fast and slow refolding reactions, as shown both by refolding assays at different times after unfolding (“double-jump” experiments) and by the formation of native cyt c in each of the fast and slow refolding reactions. Thus the fast refolding reaction is UF leads to N and the slow refolding reaction is Us leads to N, where N is native cyt c, and there is a US in equilibrium UF equilibrium in unfolded cyt c. The results are consistent with the UF in equilibrium US reaction being proline isomerization, but this has not yet been tested in detail. Folding intermediates have been detected in both reactions. In the UF leads to N reaction, the Soret absorbance change precedes the recovery of the native 695-nm band spectrum, showing that Soret absorbance monitors the formation of a folding intermediate. In the US leads to N reaction an ascorbate-reducible intermediate has been found at an early stage in folding and the Soret absorbance change occurs together with the change at 695 nm as N is formed in the final stage of folding. |
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0006-2960 |
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PMID:6261802 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3809 |
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Author |
Ryan, C.T.; Schaer, B.L.D.; Nunamaker, D.M. |
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Title |
A novel wireless data acquisition system for the measurement of hoof accelerations in the exercising horse |
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Journal Article |
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Year |
2006 |
Publication |
Equine Veterinary Journal |
Abbreviated Journal |
Equine Vet J |
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Volume |
38 |
Issue |
7 |
Pages |
671-674 |
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Keywords |
*Acceleration; Animals; Biomechanics; Equipment and Supplies/*veterinary; Hoof and Claw/*physiology; Horses/*physiology; Kinetics; Musculoskeletal Physiology; Physical Conditioning, Animal/*physiology; Running/physiology |
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REASONS FOR PERFORMING STUDY: A device is needed to safely and wirelessly evaluate accelerations experienced by the horse hoof under a variety of surface conditions with the horse exercising at training or racing speeds. OBJECTIVES: To develop a miniaturised wireless data acquisition system (WDAS) which reliably records hoof accelerations and the times over which they occur in a minimally invasive manner in the exercising Thoroughbred. METHODS: The following criteria were set for device development: production of a lightweight and minimally invasive system, which provides an adequate acceleration range, appropriate frequency response to capture high speed events, and compatibility with a low power wireless telemetry system. Following device development, the WDAS was calibrated, and tested in 6 Thoroughbred horses over a variety of surfaces. RESULTS: Collection of acceleration in seven trials using 6 horses over a variety of surfaces resulted in repeatable acceleration data with respect to the overall characteristic shape of the impact profile. Impact accelerations varied with surface, ranging 34.8-191.7 g. Accelerations on take off were in a similar range, although higher in some trials. Peak impact accelerations tended to larger over the grass paddock surface, than either the indoor arena or the dirt track. During dirt track trials, accelerations on take-off were often comparably larger than those observed on impact within the same footfall. CONCLUSIONS: This study reports the development of a wireless system that successfully measures hoof acceleration in a minimally invasive manner over a variety of surface and exercise conditions. POTENTIAL RELEVANCE: The WDAS will be used in further studies to evaluate various components of the horse-racetrack interface, in an attempt to identify risk factors for musculoskeletal injury in the Thoroughbred racehorse. |
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Richard S. Reynolds, Jr. Comparative Orthopedic Research Laboratory, Department of Clinical Studies, New Bolton Center, School of Veterinary Medicine, University of Pennsylvania, Kennett Square, Pennsylvania 19348, USA |
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0425-1644 |
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PMID:17228584 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
4023 |
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Author |
Saigo, S. |
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Title |
Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c |
Type |
Journal Article |
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Year |
1981 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
669 |
Issue |
1 |
Pages |
13-20 |
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Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism |
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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. |
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0006-3002 |
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PMID:6271238 |
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Call Number |
refbase @ user @ |
Serial |
3871 |
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Author |
Saigo, S. |
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Title |
A transient spin-state change during alkaline isomerization of ferricytochrome c |
Type |
Journal Article |
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Year |
1981 |
Publication |
Journal of Biochemistry |
Abbreviated Journal |
J Biochem (Tokyo) |
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89 |
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6 |
Pages |
1977-1980 |
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Keywords |
Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry |
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Abstract |
Kinetic difference spectra during the alkaline isomerization of ferricytochrome c were obtained by the pH-jump method in the range of 540 to 655 nm. The spectrum of the transient intermediate, which appears during the course of the isomerization, was reproduced from the spectra. The intermediate showed an intense absorption band at 600 nm, indicating that it is a high spin or mixed spin species. This is in contrast to the stable neutral and alkaline forms which are low spin species. The transient spin-state change during the isomerization was also observed upon rapid oxidation of ferrocytochrome c at alkaline pH. |
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ISSN |
0021-924X |
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PMID:6270075 |
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no |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
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Author |
Steinhoff, H.J.; Schrader, J.; Schlitter, J. |
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Title |
Temperature-jump studies and polarized absorption spectroscopy of methemoglobin-thiocyanate single crystals |
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Journal Article |
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Year |
1992 |
Publication |
Biochimica et Biophysica Acta |
Abbreviated Journal |
Biochim Biophys Acta |
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Volume |
1121 |
Issue |
3 |
Pages |
269-278 |
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Animals; Crystallization; Horses; Kinetics; Methemoglobin/*chemistry; Solutions; Spectrum Analysis; Temperature; Thiocyanates/*chemistry |
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Abstract |
Association equilibria and association kinetics of the thiocyanate binding reaction to methemoglobin in single crystals and solution are studied using temperature-jump technique and polarized absorption spectroscopy. Different kinetic constants are found for the reaction in solution and crystal phase for the alpha- and beta-subunits of the methemoglobin tetramer. The reduction of the reactivity of the alpha- and beta-subunits in crystalline phase is 6-fold and 2.4-fold, respectively, compared to the values found in solution. The intramolecular binding reaction of the N epsilon of the distal histidine E7 which is observed in methemoglobin in solution cannot be detected in single crystals. Our results suggest that crystallization of hemoglobin has little influence on small-scale structural fluctuations which are necessary for ligands to get to the binding sites and large-scale structural motions are suppressed. |
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Institut fur Biophysik, Ruhr-Universitat Bochum, Germany |
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0006-3002 |
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PMID:1627604 |
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no |
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Equine Behaviour @ team @ |
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3800 |
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Author |
Sukhomlinov, B.F.; Korobov, V.N.; Gonchar, M.V.; Datsiuk, L.A.; Korzhev, V.A. |
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Title |
[Comparative analysis of the peroxidase activity of myoglobins in mammals] |
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Journal Article |
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Year |
1987 |
Publication |
Zhurnal Evoliutsionnoi Biokhimii i Fiziologii |
Abbreviated Journal |
Zh Evol Biokhim Fiziol |
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23 |
Issue |
1 |
Pages |
37-41 |
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Amino Acid Sequence; Animals; Ecology; *Evolution; Kinetics; Mammals/*metabolism; Myoglobin/*metabolism; Peroxidases/*metabolism |
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Studies have been made on the peroxidase activity of metmyoglobins in animals from various ecological groups--the horse Equus caballus, cattle Bos taurus, beaver Castor fiber, otter Lutra lutra, mink Mustela vison and dog Canis familiaris. It was found that the level of this activity in diving animals depends on the duration of their diving, whereas in terrestrial species--on the strength of muscular contraction. |
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Russian |
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Sravnitel'nyi analiz peroksidaznoi aktivnosti mioglobinov u mlekopitaiushchikh |
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0044-4529 |
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PMID:3564776 |
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Equine Behaviour @ team @ |
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2681 |
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Author |
Touma, C.; Sachser, N.; Mostl, E.; Palme, R. |
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Title |
Effects of sex and time of day on metabolism and excretion of corticosterone in urine and feces of mice |
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Journal Article |
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Year |
2003 |
Publication |
General and Comparative Endocrinology |
Abbreviated Journal |
Gen Comp Endocrinol |
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Volume |
130 |
Issue |
3 |
Pages |
267-278 |
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Animals; Chromatography, High Pressure Liquid; Circadian Rhythm/*physiology; Corticosterone/*metabolism/urine; Feces/*chemistry; Female; Immunoenzyme Techniques; Kinetics; Male; Mice; Mice, Inbred C57BL; Reference Values; Sex Factors; Stress/metabolism; Time Factors; Tritium |
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Non-invasive techniques to monitor stress hormones in small animals like mice offer several advantages and are highly demanded in laboratory as well as in field research. Since knowledge about the species-specific metabolism and excretion of glucocorticoids is essential to develop such a technique, we conducted radiometabolism studies in mice (Mus musculus f. domesticus, strain C57BL/6J). Each mouse was injected intraperitoneally with 740 kBq of 3H-labelled corticosterone and all voided urine and fecal samples were collected for five days. In a first experiment 16 animals (eight of each sex) received the injection at 9 a.m., while eight mice (four of each sex) were injected at 9 p.m. in a second experiment. In both experiments radioactive metabolites were recovered predominantly in the feces, although males excreted significantly higher proportions via the feces (about 73%) than females (about 53%). Peak radioactivity in the urine was detected within about 2h after injection, while in the feces peak concentrations were observed later (depending on the time of injection: about 10h postinjection in experiment 1 and about 4h postinjection in experiment 2, thus proving an effect of the time of day). The number and relative abundance of fecal [3H]corticosterone metabolites was determined by high performance liquid chromatography (HPLC). The HPLC separations revealed that corticosterone was extensively metabolized mainly to more polar substances. Regarding the types of metabolites formed, significant differences were found between males and females, but not between the experiments. Additionally, the immunoreactivity of these metabolites was assessed by screening the HPLC fractions with four enzyme immunoassays (EIA). However, only a newly established EIA for 5alpha-pregnane-3beta,11beta,21-triol-20-one (measuring corticosterone metabolites with a 5alpha-3beta,11beta-diol structure) detected several peaks of radioactive metabolites with high intensity in both sexes, while the other EIAs showed only minor immunoreactivity. Thus, our study for the first time provides substantial information about metabolism and excretion of corticosterone in urine and feces of mice and is the first demonstrating a significant impact of the animals' sex and the time of day. Based on these data it should be possible to monitor adrenocortical activity non-invasively in this species by measuring fecal corticosterone metabolites with the newly developed EIA. Since mice are extensively used in research world-wide, this could open new perspectives in various fields from ecology to behavioral endocrinology. |
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Department of Behavioral Biology, Institute of Neuro and Behavioral Biology, University of Muenster, Badestrasse 9, D-48149 Muenster, Germany. touma@uni-muenster.de |
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0016-6480 |
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PMID:12606269 |
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Equine Behaviour @ team @ |
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4086 |
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Author |
Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. |
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Title |
A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) |
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Journal Article |
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Year |
1977 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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77 |
Issue |
1 |
Pages |
193-199 |
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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 |
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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. |
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0014-2956 |
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PMID:20304 |
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Equine Behaviour @ team @ |
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3814 |
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Author |
Wilson, M.T.; Silvestrini, M.C.; Morpurgo, L.; Brunori, M. |
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Title |
Electron transfer kinetics between Rhus vernicifera stellacyanin and cytochrome c (horse heart cytochrome c and Pseudomonas cytochrome c551) |
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Journal Article |
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Year |
1979 |
Publication |
Journal of Inorganic Biochemistry |
Abbreviated Journal |
J Inorg Biochem |
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11 |
Issue |
2 |
Pages |
95-100 |
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Keywords |
Animals; Copper; Cytochrome c Group/*metabolism; Electron Transport; Kinetics; Metalloproteins/*metabolism; Plant Proteins/*metabolism; *Plants, Toxic; Pseudomonas aeruginosa/*metabolism; Toxicodendron/*metabolism |
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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. |
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Series Title |
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Abbreviated Series Title |
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|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
0162-0134 |
ISBN |
|
Medium |
|
|
| |
Area |
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Expedition |
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Conference |
|
|
| |
Notes |
PMID:228006 |
Approved |
no |
|
| |
Call Number |
refbase @ user @ |
Serial |
3879 |
|
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