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Author |
Andersen, N.H.; Norgaard, A.; Jensen, T.J.; Ulstrup, J. |
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Title |
Sequential unfolding of the two-domain protein Pseudomonas stutzeri cytochrome c4 |
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2002 |
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Journal of Inorganic Biochemistry |
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88 |
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3-4 |
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316-327 |
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P. stutzeri cytochrome c4; Sequential unfolding; Di-haem protein; Unfolding |
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P. stutzeri cytochrome c4 is a di-haem protein, composed of two globular domains each with His-Met coordinated haem, and a hydrogen bond network between the domains. The domain foldings are highly symmetric but with specific differences including structural differences of ligand coordination, and different spin states of the oxidised haem groups. We have studied unfolding of oxidised P. stutzeri cyt c4 induced thermally and by chemical denaturants. Horse heart cyt c was a reference molecule. Isothermal unfolding induced by guanidinium chloride and acid was followed by Soret, α/β, and 701-nm band absorption, and by far-UV circular dichroism spectroscopy. Multifarious patterns emerge, but the two domains clearly unfold sequentially. One phase, assigned to unfolding of the N-terminal domain, proceeds at guanidinium concentrations up to [approximate]1.0 M. This is followed by two overlapping phases at higher concentrations. The intermediate state maintains Fe-Met coordination, assigned to the C-terminal domain. Interdomain interaction is reflected in decreasing values of the cooperativity parameters. Differential scanning calorimetry shows a single peak, but two peaks appear when guanidinium chloride up to 0.4 M is present. This reflects different chemical action in chemical and thermal unfolding. Acid-induced unfolding kinetics was addressed by pH jumps using diode array stopped-flow techniques. Three kinetic phases in the 701 nm Fe-Met marker band, and four phases in the Soret and α/β bands, spanning 4-1000 ms could be distinguished on pH jumps from 7.5 to the range 2.5-3.5. In this range of time and pH cyt c appears to unfold in no more than two phases. Spectral properties of the kinetic intermediates could be identified. Sequential domain unfolding, formation of high-spin states, and an intermediate state with Fe-Met coordination to a single haem group are features of the unfolding kinetics. |
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3973 |
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Author |
Kihara, H. |
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Title |
Comparison of the redox reactions of various types of cytochrome c with iron hexacyanides |
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1981 |
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Biochimica et Biophysica Acta (BBA) – Bioenergetics |
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634 |
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93-104 |
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Cytochrome c; Redox reaction; Iron hexacyanide; Temperature jump; Electron transfer |
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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. |
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3980 |
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Kesel, L.; Neil, D.H. |
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Restraint and handling of animals |
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1998 |
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Clinical Textbook for Veterinary Technicians. 4th ed. |
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1-26 |
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Cited By (since 1996): 1; Export Date: 21 October 2008 |
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Equine Behaviour @ team @ |
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4523 |
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Luescher, U.A.; McKeown, D.B.; Dean, H. |
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A cross-sectional study on compulsive behaviour (stable vices) in horses |
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1998 |
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Equine veterinary journal. Supplement |
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27 |
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14-18 |
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Cited By (since 1996): 22; Export Date: 21 October 2008 |
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Equine Behaviour @ team @ |
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4527 |
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Waring, G.H. |
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2003 |
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Horse behavior. 2nd ed |
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442 pp |
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Cited By (since 1996): 1; Export Date: 21 October 2008 |
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Equine Behaviour @ team @ |
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4548 |
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Clutton-Brock, T.H.; Guinness, F.E.; Albon, S.D. |
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Red Deer: The Behavior and Ecology of Two Sexes |
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1982 |
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Equine Behaviour @ team @ |
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4886 |
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Kummer, H. |
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Social Organisation of Hamadryas Baboons |
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1968 |
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Equine Behaviour @ team @ |
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4887 |
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Chapron, G.; Kaczensky, P.; Linnell, J.D.C.; Arx, M.; Huber, D.; Andrén, H. |
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Recovery of large carnivores in Europe's modern human-dominated landscapes |
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2014 |
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Science |
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346 |
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Equine Behaviour @ team @ Chapron2014 |
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6451 |
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Fritts, S.H.; Bangs, E.E.; Gore, J.F. |
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The relationship of wolf recovery to habitat conservation and biodiversity in the northwestern United States |
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1994 |
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Landsc Urban Plan |
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Equine Behaviour @ team @ Fritts1994 |
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6453 |
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Pimlott, D.H. |
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The use of tape-recorded wolf howls to locate timber wolves |
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1960 |
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Twenty-second Midwest Wildlife Congress |
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Toronto |
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Equine Behaviour @ team @ Pimlott1960 |
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6454 |
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