Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 Nov;71(11):4303–4306. doi: 10.1073/pnas.71.11.4303

Proton Magnetic Resonance Spectra of Rhodospirillum rubrum Cytochrome C2

Gary M Smith 1, Martin D Kamen 1
PMCID: PMC433870  PMID: 4373707

Abstract

Nuclear magnetic resonance spectra of ferro- and ferricytochrome C2 from the facultative photoheterotroph, Rhodospirillum rubrum, obtained with a 220-MHz spectrometer, are presented. Assignments to protons of various important structural groups in contact with or near the prosthetic heme group are given. These include (a) in the ferro-form, methyl, cβ and cγ protons of the extraplanar ligand residue, methionine 91, and methyl protons of the residue leucine 32; and (b) corresponding protons in the ferri-form with the addition of methyl protons from the condensation of a heme vinyl group with cysteine 17, a single proton from the condensation involving cysteine 14, and protons from the ring methyls. These resonances are compared with those corresponding to the same groups in horse heart cytochrome c.

Keywords: nuclear magnetic resonance assignments, cytochromes c, comparative structures

Full text

PDF
4303

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Davis K. A., Hatefi Y., Salemme F. R., Kamen M. D. Enzymic redox reactions of cytochromes c. Biochem Biophys Res Commun. 1972 Dec 4;49(5):1329–1335. doi: 10.1016/0006-291x(72)90612-2. [DOI] [PubMed] [Google Scholar]
  2. Dickerson R. E. Sequence and structure homologies in bacterial and mammalian-type cytochromes. J Mol Biol. 1971 Apr 14;57(1):1–15. doi: 10.1016/0022-2836(71)90116-1. [DOI] [PubMed] [Google Scholar]
  3. Dickerson R. E., Takano T., Eisenberg D., Kallai O. B., Samson L., Cooper A., Margoliash E. Ferricytochrome c. I. General features of the horse and bonito proteins at 2.8 A resolution. J Biol Chem. 1971 Mar 10;246(5):1511–1535. [PubMed] [Google Scholar]
  4. Dus K., Sletten K., Kamen M. D. Cytochrome c2 of Rhodospirillum rubrum. II. Complete amino acid sequence and phylogenetic relationships. J Biol Chem. 1968 Oct 25;243(20):5507–5518. [PubMed] [Google Scholar]
  5. Fanger M. W., Hettinger T. P., Harbury H. A. Pseudomonas cytochrome c. II. Effect of modification of the methionine residues. Biochemistry. 1967 Mar;6(3):713–720. doi: 10.1021/bi00855a010. [DOI] [PubMed] [Google Scholar]
  6. Giessner-Prettre C., Pullman B. Intermolecular nuclear shielding due to the aromatic amino acids of proteins and to porphyrins. J Theor Biol. 1971 May;31(2):287–294. doi: 10.1016/0022-5193(71)90188-3. [DOI] [PubMed] [Google Scholar]
  7. Greenwood C., Wilson M. T. 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. doi: 10.1111/j.1432-1033.1971.tb01507.x. [DOI] [PubMed] [Google Scholar]
  8. Gupta R. K., Koenig S. H. Some aspects of pH and temperature dependence of the NMR spectra of cytochrome C. Biochem Biophys Res Commun. 1971 Dec 3;45(5):1134–1143. doi: 10.1016/0006-291x(71)90137-9. [DOI] [PubMed] [Google Scholar]
  9. Gupta R. K., Redfield A. G. NMR double resonance study of azidoferricytochrome C. Biochem Biophys Res Commun. 1970 Oct 23;41(2):273–281. doi: 10.1016/0006-291x(70)90499-7. [DOI] [PubMed] [Google Scholar]
  10. HORIO T., HIGASHI T., SASAGAWA M., KUSAI K., NAKAI M., OKUNUKI K. Preparation of crystalline Pseudomonas cvtochrome c-551 and its general properties. Biochem J. 1960 Oct;77:194–201. doi: 10.1042/bj0770194. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Harbury H. A., Cronin J. R., Fanger M. W., Hettinger T. P., Murphy A. J., Myer Y. P., Vinogradov S. N. Complex formation between methionine and a heme peptide from cytochrome c. Proc Natl Acad Sci U S A. 1965 Dec;54(6):1658–1664. doi: 10.1073/pnas.54.6.1658. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Horio T., Kamen M. D. Bacterial cytochromes. II. Functional aspects. Annu Rev Microbiol. 1970;24:399–428. doi: 10.1146/annurev.mi.24.100170.002151. [DOI] [PubMed] [Google Scholar]
  13. Keller R. M., Pettigrew G. W., Wüthrich K. Structural studies by proton NMR of cytochrome C-557 from Crithidia oncopelti. FEBS Lett. 1973 Oct 15;36(2):151–156. doi: 10.1016/0014-5793(73)80358-8. [DOI] [PubMed] [Google Scholar]
  14. Keller R. M., Wüthrich K. The electronic g-tensor in cytochrome b5: high resolution proton magnetic resonance studies. Biochim Biophys Acta. 1972 Dec 28;285(2):326–336. doi: 10.1016/0005-2795(72)90317-0. [DOI] [PubMed] [Google Scholar]
  15. Krejcarek G. E., Turner L., Dus K. Investigation of photosynthetic cytochromes c by high resolution NMR spectroscopy. Biochem Biophys Res Commun. 1971 Mar 5;42(5):983–991. doi: 10.1016/0006-291x(71)90527-4. [DOI] [PubMed] [Google Scholar]
  16. Mailer C., Taylor C. P. Electron paramagnetic resonance study of single crystals of horse heart ferricytochrome c at 4.2 degrees K. Can J Biochem. 1972 Oct;50(10):1048–1055. doi: 10.1139/o72-145. [DOI] [PubMed] [Google Scholar]
  17. McArdle J. V., Gray H. B., Creutz C., Sutin N. Kinetic studies of the oxidation of ferrocytochrome c from horse heart and Candida krusei by tris(1,10-phenanthroline)cobalt(3). J Am Chem Soc. 1974 Sep 4;96(18):5737–5741. doi: 10.1021/ja00825a009. [DOI] [PubMed] [Google Scholar]
  18. McDonald C. C., Phillips W. D., LeGall J. Proton magnetic resonance studies of Desulfovibrio cytochromes c3. Biochemistry. 1974 Apr 23;13(9):1952–1959. doi: 10.1021/bi00706a027. [DOI] [PubMed] [Google Scholar]
  19. McDonald C. C., Phillips W. D. Proton magnetic resonance studies of horse cytochrome c. Biochemistry. 1973 Aug 14;12(17):3170–3186. doi: 10.1021/bi00741a006. [DOI] [PubMed] [Google Scholar]
  20. Redfield A. G., Gupta R. K. Pulsed NMR study of the structure of cytochrome c. Cold Spring Harb Symp Quant Biol. 1972;36:405–411. doi: 10.1101/sqb.1972.036.01.052. [DOI] [PubMed] [Google Scholar]
  21. Roberts G. C., Jardetzky O. Nuclear magnetic resonance spectroscopy of amino acids, peptides, and proteins. Adv Protein Chem. 1970;24:447–545. doi: 10.1016/s0065-3233(08)60246-6. [DOI] [PubMed] [Google Scholar]
  22. Salemme F. R., Freer S. T., Xuong N. H., Alden R. A., Kraut J. The structure of oxidized cytochrome c 2 of Rhodospirillum rubrum. J Biol Chem. 1973 Jun 10;248(11):3910–3921. doi: 10.2210/pdb1c2c/pdb. [DOI] [PubMed] [Google Scholar]
  23. Salemme F. R., Kraut J., Kamen M. D. Structural bases for function in cytochromes c. An interpretation of comparative x-ray and biochemical data. J Biol Chem. 1973 Nov 25;248(22):7701–7716. [PubMed] [Google Scholar]
  24. Shulman R. G., Glarum S. H., Karplus M. Electronic structure of cyanide complexes of hemes and heme proteins. J Mol Biol. 1971 Apr 14;57(1):93–115. doi: 10.1016/0022-2836(71)90121-5. [DOI] [PubMed] [Google Scholar]
  25. Shulman R. G., Wüthrich K., Yamane T., Antonini E., Brunori M. Nuclear magnetic resonances of reconstituted myoglobins. Proc Natl Acad Sci U S A. 1969 Jul;63(3):623–628. doi: 10.1073/pnas.63.3.623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Smith W. R., Jr, Sybesma C., Litchfield W. J., Dus K. Photochemical systems of Rhodospirillum rubrum. Light-induced reactions and biological functions of c-type cytochromes in relation to P-870. Biochemistry. 1973 Jul 3;12(14):2665–2671. doi: 10.1021/bi00738a018. [DOI] [PubMed] [Google Scholar]
  27. Stellwagen E., Shulman R. G. Nuclear magnetic resonance study of the rate of electron transfer between cytochrome c and iron hexacyanides. J Mol Biol. 1973 Nov 15;80(4):559–573. doi: 10.1016/0022-2836(73)90197-6. [DOI] [PubMed] [Google Scholar]
  28. Takano T., Kallai O. B., Swanson R., Dickerson R. E. The structure of ferrocytochrome c at 2.45 A resolution. J Biol Chem. 1973 Aug 10;248(15):5234–5255. [PubMed] [Google Scholar]
  29. VERNON L. P., KAMEN M. D. Hematin compounds in photosynthetic bacteria. J Biol Chem. 1954 Dec;211(2):643–662. [PubMed] [Google Scholar]
  30. Wüthrich K. High-resolution proton nuclear magnetic resonance spectroscopy of cytochrome. Proc Natl Acad Sci U S A. 1969 Aug;63(4):1071–1078. doi: 10.1073/pnas.63.4.1071. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES