FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Biochem J / Identification of the ligand-exchange process in the alkalin...
The Biochemical journal1987; 246(1); 43-54; doi: 10.1042/bj2460043

Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c.

Abstract: Magnetic-circular-dichroism (m.c.d.) spectra over the wavelength range 300-2000 nm at room temperature and at 4.2K of horse heart cytochrome c are reported at a series of pH values between 7.8 and 11.0, encompassing the alkaline transition. The effect of glassing agents on the e.p.r. spectrum at various pH values is also reported. Comparison of these results with spectra obtained for the n-butylamine adduct of soybean leghaemoglobin support the hypothesis that lysine is the sixth ligand in the alkaline form of horse heart cytochrome c. The m.c.d. and e.p.r. spectra of horse heart cytochrome c in the presence of 1-methylimidazole have also been examined. These studies strongly suggest that histidine-18, the proximal ligand of the haem, is the ionizing group that triggers the alkaline transition. Low-temperature m.c.d. and e.p.r. spectra are also reported for Pseudomonas aeruginosa cytochrome c551. It is shown that no ligand exchange takes place at the haem in this species over the pH range 6.0-11.3.
Get Full Text
Publication Date: 1987-08-15 PubMed ID: 2823795PubMed Central: PMC1148238DOI: 10.1042/bj2460043Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • Journal Article
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research investigates the ligand-exchange process in the alkaline transition of horse heart cytochrome c, examining the impacts of pH on magnetic-circular-dichroism (m.c.d.) spectra. The findings strongly suggest that histidine-18 is the triggering group for this transition.

Understanding Cytochrome C and Ligand-Exchange Process

  • The research revolves around Cytochrome c, a small protein found in many living organisms, which plays a crucial role in the process of cellular respiration.
  • It is involved in the transport of electrons during the production of energy in cells.
  • The “ligand-exchange process” refers to the swapping of one ligand (an ion or molecule that binds to a central atom to form a coordination complex) for another within a molecule.

Methodology and Experiments

  • The team conducted a survey of magnetic-circular-dichroism (m.c.d.) spectra over the wavelength range 300-2000 nm at room temperature and at 4.2K for horse heart cytochrome c at various pH levels (7.8 to 11.0).
  • They compared the effects of different glassing agents on the electron paramagnetic resonance (e.p.r.) spectrum at these pH levels.
  • The results were then compared with spectra obtained for the n-butylamine adduct of soybean leghaemoglobin, aiding in the hypothesis that lysine is the sixth ligand in the alkaline form of horse heart cytochrome c.
  • The team also studied the m.c.d. and e.p.r. spectra of horse heart cytochrome c in the presence of 1-methylimidazole.

Key Findings

  • These investigations strongly suggest that histidine-18 is the proximal ligand of the haem (an iron-containing compound that forms the non-protein part of certain enzymes) and is responsible for triggering the alkaline transition.
  • In contrast, the research observed that no ligand exchange occurs in the haem of Pseudomonas aeruginosa cytochrome c551 over the pH range 6.0-11.3, showing a diverse range of reactions in different species.

Cite This Article

APA
Gadsby PM, Peterson J, Foote N, Greenwood C, Thomson AJ. (1987). Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c. Biochem J, 246(1), 43-54. https://doi.org/10.1042/bj2460043

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 246
Issue: 1
Pages: 43-54

Researcher Affiliations

Gadsby, P M
  • School of Chemical Sciences, University of East Anglia, Norwich, U.K.
Peterson, J
    Foote, N
      Greenwood, C
        Thomson, A J

          MeSH Terms

          • Animals
          • Bacterial Proteins
          • Circular Dichroism
          • Cytochrome c Group
          • Electron Spin Resonance Spectroscopy
          • Horses
          • Hydrogen-Ion Concentration
          • Imidazoles
          • Ligands
          • Myocardium / enzymology
          • Pseudomonas aeruginosa / analysis
          • Temperature

          References

          This article includes 34 references
          1. Greenwood C, Palmer G. Evidence for the existence of two functionally distinct forms cytochrome c manomer at alkaline pH.. J Biol Chem 1965 Sep;240(9):3660-3.
            pubmed: 5835945
          2. Foote N, Peterson J, Gadsby PM, Greenwood C, Thomson AJ. A study of the oxidized form of Pseudomonas aeruginosa cytochrome c-551 peroxidase with the use of magnetic circular dichroism.. Biochem J 1984 Oct 15;223(2):369-78.
            pubmed: 6093773doi: 10.1042/bj2230369google scholar: lookup
          3. Margoliash E, Schejter A. Cytochrome c.. Adv Protein Chem 1966;21:113-286.
            pubmed: 5333288doi: 10.1016/s0065-3233(08)60128-xgoogle scholar: lookup
          4. Salmeen I, Palmer G. Electron paramagnetic resonance of beef-heart ferricytochrome c.. J Chem Phys 1968 Mar 1;48(5):2049-52.
            pubmed: 4297179doi: 10.1063/1.1669014google scholar: lookup
          5. Greenwood C, Wilson MT. Studies on ferricytochrome c. I. Effect of pH, ionic strength and protein denaturants on the spectra of ferricytochrome c.. Eur J Biochem 1971 Sep 13;22(1):5-10.
            pubmed: 5099216doi: 10.1111/j.1432-1033.1971.tb01507.xgoogle scholar: lookup
          6. Gupta RK, Koenig SH. Some aspects of pH and temperature dependence of the NMR spectra of cytochrome C.. Biochem Biophys Res Commun 1971 Dec 3;45(5):1134-43.
            pubmed: 5167489doi: 10.1016/0006-291x(71)90137-9google scholar: lookup
          7. Lambeth DO, Campbell KL, Zand R, Palmer G. The appearance of transient species of cytochrome c upon rapid oxidation or reduction at alkaline pH.. J Biol Chem 1973 Dec 10;248(23):8130-6.
            pubmed: 4356619
          8. Davis LA, Schejter A, Hess GP. Alkaline isomerization of oxidized cytochrome c. Equilibrium and kinetic measurements.. J Biol Chem 1974 Apr 25;249(8):2624-32.
            pubmed: 4362690
          9. Wilgus H, Stellwagen E. Alkaline isomerization of ferricytochrome c: identification of the lysine ligand.. Proc Natl Acad Sci U S A 1974 Jul;71(7):2892-4.
            pubmed: 4368392doi: 10.1073/pnas.71.7.2892google scholar: lookup
          10. Wittenberg JB. Facilitated oxygen diffusion. The role of leghemoglobin in nitrogen fixation by bacteroids isolated from soybean root nodules.. J Biol Chem 1974 Jul 10;249(13):4057-66.
            pubmed: 4859329
          11. Stellwagen E, Babul J, Wilgus H. The alkaline isomerization of lysine-modified ferricytochrome c.. Biochim Biophys Acta 1975 Sep 9;405(1):115-21.
            pubmed: 240434doi: 10.1016/0005-2795(75)90321-9google scholar: lookup
          12. Mathews FS. The structure, function and evolution of cytochromes.. Prog Biophys Mol Biol 1985;45(1):1-56.
            pubmed: 3881803doi: 10.1016/0079-6107(85)90004-5google scholar: lookup
          13. Moore GR, Williams RJ, Peterson J, Thomson AJ, Mathews FS. A spectroscopic investigation of the structure and redox properties of Escherichia coli cytochrome b-562.. Biochim Biophys Acta 1985 May 20;829(1):83-96.
            pubmed: 2986699doi: 10.1016/0167-4838(85)90071-8google scholar: lookup
          14. Thomson AJ, Greenwood C, Gadsby PM, Peterson J, Eglinton DG, Hill BC, Nicholls P. The structure of the cytochrome a3-CuB site of mammalian cytochrome c oxidase as probed by MCD and EPR spectroscopy.. J Inorg Biochem 1985 Mar-Apr;23(3-4):187-97.
            pubmed: 2991457doi: 10.1016/0162-0134(85)85025-xgoogle scholar: lookup
          15. Pettigrew GW, Aviram I, Schejter A. The role of the lysines in the alkaline heme-linked ionization of ferric cytochrome c.. Biochem Biophys Res Commun 1976 Feb 9;68(3):807-13.
            pubmed: 4069doi: 10.1016/0006-291x(76)91217-1google scholar: lookup
          16. Kihara H, Saigo S, Nakatani H, Hiromi K, Ikeda-Saito M, Iizuka T. Kinetic study of isomerization of ferricytochrome c at alkaline pH.. Biochim Biophys Acta 1976 May 14;430(2):225-43.
            pubmed: 6059doi: 10.1016/0005-2728(76)90081-5google scholar: lookup
          17. Parr SR, Barber D, Greenwood C. A purification procedure for the soluble cytochrome oxidase and some other respiratory proteins from Pseudomonas aeruginosa.. Biochem J 1976 Aug 1;157(2):423-30.
            pubmed: 183750doi: 10.1042/bj1570423google scholar: lookup
          18. Brautigan DL, Feinberg BA, Hoffman BM, Margoliash E, Preisach J, Blumberg WE. Multiple low spin forms of the cytochrome c ferrihemochrome. EPR spectra of various eukaryotic and prokaryotic cytochromes c.. J Biol Chem 1977 Jan 25;252(2):574-82.
            pubmed: 13072
          19. Rawlings J, Stephens PJ, Nafie LA, Kamen MD. Near-infrared magnetic circular dichroism of cytochrome c'.. Biochemistry 1977 Apr 19;16(8):1725-9.
            pubmed: 192272doi: 10.1021/bi00627a032google scholar: lookup
          20. Kitagawa T, Ozaki Y, Teraoka J, Kyogoku Y, Yamanaka T. The pH dependence of the resonance raman spectra and structural alterations at heme moieties of various c-type cytochromes.. Biochim Biophys Acta 1977 Sep 27;494(1):100-14.
            pubmed: 20152doi: 10.1016/0005-2795(77)90138-6google scholar: lookup
          21. Siedow JN, Power S, de la Rosa FF, Palmer G. The preparation and characterization of highly purified, enzymically active complex III from baker's yeast.. J Biol Chem 1978 Apr 10;253(7):2392-9.
            pubmed: 204648
          22. Myer YP, Bullock PA. Cytochrome b562 from Escherichia coli: conformational, configurational, and spin-state characterization.. Biochemistry 1978 Sep 5;17(18):3723-9.
            pubmed: 359043doi: 10.1021/bi00611a008google scholar: lookup
          23. Keller RM, Wüthrich K. Evolutionary change of the heme c electronic structure: ferricytochrome c-551 from Pseudomonas aeruginosa and horse heart ferricytochrome c.. Biochem Biophys Res Commun 1978 Aug 14;83(3):1132-9.
            pubmed: 213063doi: 10.1016/0006-291x(78)91513-9google scholar: lookup
          24. Adman ET. A comparison of the structures of electron transfer proteins.. Biochim Biophys Acta 1979 Aug 17;549(2):107-44.
            pubmed: 224921doi: 10.1016/0304-4173(79)90012-0google scholar: lookup
          25. Smith HT, Millett F. Involvement of lysines-72 and -79 in the alkaline isomerization of horse heart ferricytochrome c.. Biochemistry 1980 Mar 18;19(6):1117-20.
            pubmed: 6245678doi: 10.1021/bi00547a012google scholar: lookup
          26. Moore GR, Pettigrew GW, Pitt RC, Williams RJ. pH dependence of the redox potential of Pseudomonas aeruginosa cytochrome c-551.. Biochim Biophys Acta 1980 Apr 2;590(2):261-71.
            pubmed: 6245686doi: 10.1016/0005-2728(80)90030-4google scholar: lookup
          27. O'Keeffe DT, Anthony C. The interaction between methanol dehydrogenase and the autoreducible cytochromes c of the facultative methylotroph Pseudomonas AM1.. Biochem J 1980 Aug 15;190(2):481-4.
            pubmed: 6258570doi: 10.1042/bj1900481google scholar: lookup
          28. Saigo S. A transient spin-state change during alkaline isomerization of ferricytochrome c.. J Biochem 1981 Jun;89(6):1977-80.
            pubmed: 6270075doi: 10.1093/oxfordjournals.jbchem.a133400google scholar: lookup
          29. Wooten JB, Cohen JS, Vig I, Schejter A. pH-induced conformational transitions of ferricytochrome c: a carbon-13 and deuterium nuclear magnetic resonance study.. Biochemistry 1981 Sep 15;20(19):5394-402.
            pubmed: 6271186doi: 10.1021/bi00522a007google scholar: lookup
          30. Bosshard HR. Alkaline isomerization of ferricytochrome c: lysine is not replacing methionine at the sixth co-ordination site of the haem iron.. J Mol Biol 1981 Dec 25;153(4):1125-49.
            pubmed: 6283086doi: 10.1016/0022-2836(81)90471-xgoogle scholar: lookup
          31. Matsuura Y, Takano T, Dickerson RE. Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 A resolution and comparison of the two redox forms.. J Mol Biol 1982 Apr 5;156(2):389-409.
            pubmed: 6283101doi: 10.1016/0022-2836(82)90335-7google scholar: lookup
          32. Eglinton DG, Gadsby PM, Sievers G, Peterson J, Thomson AJ. A comparative study of the low-temperature magnetic circular dichroism spectra of horse heart metmyoglobin and bovine liver catalase derivatives.. Biochim Biophys Acta 1983 Feb 15;742(3):648-58.
            pubmed: 6838894doi: 10.1016/0167-4838(83)90284-4google scholar: lookup
          33. Salerno JC. Cytochrome electron spin resonance line shapes, ligand fields, and components stoichiometry in ubiquinol-cytochrome c oxidoreductase.. J Biol Chem 1984 Feb 25;259(4):2331-6.
            pubmed: 6321467
          34. Brandt KG, Parks PC, Czerlinski GH, Hess GP. On the elucidation of the pH dependence of the oxidation-reduction potential of cytochrome c at alkaline pH.. J Biol Chem 1966 Sep 25;241(18):4180-5.
            pubmed: 4958912

          Citations

          This article has been cited 18 times.
          Subscribe to our newsletter
          Join 99,030 horse owners like you who receive our email updates on horse health and nutrition.