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. 1999 May;8(5):947–957. doi: 10.1110/ps.8.5.947

Auracyanin A from the thermophilic green gliding photosynthetic bacterium Chloroflexus aurantiacus represents an unusual class of small blue copper proteins.

G Van Driessche 1, W Hu 1, G Van de Werken 1, F Selvaraj 1, J D McManus 1, R E Blankenship 1, J J Van Beeumen 1
PMCID: PMC2144333  PMID: 10338005

Abstract

The amino acid sequence of the small copper protein auracyanin A isolated from the thermophilic photosynthetic green bacterium Chloroflexus aurantiacus has been determined to be a polypeptide of 139 residues. His58, Cys123, His128, and Met132 are spaced in a way to be expected if they are the evolutionary conserved metal ligands as in the known small copper proteins plastocyanin and azurin. Secondary structure prediction also indicates that auracyanin has a general beta-barrel structure similar to that of azurin from Pseudomonas aeruginosa and plastocyanin from poplar leaves. However, auracyanin appears to have sequence characteristics of both small copper protein sequence classes. The overall similarity with a consensus sequence of azurin is roughly the same as that with a consensus sequence of plastocyanin, namely 30.5%. We suggest that auracyanin A, together with the B forms, is the first example of a new class of small copper proteins that may be descendants of an ancestral sequence to both the azurin proteins occurring in prokaryotic nonphotosynthetic bacteria and the plastocyanin proteins occurring in both prokaryotic cyanobacteria and eukaryotic algae and plants. The N-terminal sequence region 1-18 of auracyanin is remarkably rich in glycine and hydroxy amino acids, and required mass spectrometric analysis to be determined. The nature of the blocking group X is not yet known, although its mass has been determined to be 220 Da. The auracyanins are the first small blue copper proteins found and studied in anoxygenic photosynthetic bacteria and are likely to mediate electron transfer between the cytochrome bc1 complex and the photosynthetic reaction center.

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Selected References

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  1. Ambler R. P. Sequence variability in bacterial cytochromes c. Biochim Biophys Acta. 1991 May 23;1058(1):42–47. doi: 10.1016/s0005-2728(05)80266-x. [DOI] [PubMed] [Google Scholar]
  2. Ambler R. P., Tobari J. The primary structures of Pseudomonas AM1 amicyanin and pseudoazurin. Two new sequence classes of blue copper proteins. Biochem J. 1985 Dec 1;232(2):451–457. doi: 10.1042/bj2320451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. André E., Kessler M., Briquel M. E., Alexandre P., Hurault de Ligny B., Huriet C. Intérêt pratique du dosage des produits de dégradation de la fibrine urinaire dans la surveillance précoce des transplantés rénaux. Pathol Biol (Paris) 1983 Jan;31(1):23–27. [PubMed] [Google Scholar]
  4. Biemann K. Appendix 5. Nomenclature for peptide fragment ions (positive ions). Methods Enzymol. 1990;193:886–887. doi: 10.1016/0076-6879(90)93460-3. [DOI] [PubMed] [Google Scholar]
  5. Blankenship R. E. Origin and early evolution of photosynthesis. Photosynth Res. 1992;33:91–111. [PubMed] [Google Scholar]
  6. Blankenship R. E. Protein structure, electron transfer and evolution of prokaryotic photosynthetic reaction centers. Antonie Van Leeuwenhoek. 1994;65(4):311–329. doi: 10.1007/BF00872216. [DOI] [PubMed] [Google Scholar]
  7. Bruschi M., Guerlesquin F. Structure, function and evolution of bacterial ferredoxins. FEMS Microbiol Rev. 1988 Apr-Jun;4(2):155–175. doi: 10.1111/j.1574-6968.1988.tb02741.x. [DOI] [PubMed] [Google Scholar]
  8. CRESTFIELD A. M., MOORE S., STEIN W. H. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J Biol Chem. 1963 Feb;238:622–627. [PubMed] [Google Scholar]
  9. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  10. Condit C. M., Meagher R. B. Expression of a gene encoding a glycine-rich protein in petunia. Mol Cell Biol. 1987 Dec;7(12):4273–4279. doi: 10.1128/mcb.7.12.4273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Durley R., Chen L., Lim L. W., Mathews F. S., Davidson V. L. Crystal structure analysis of amicyanin and apoamicyanin from Paracoccus denitrificans at 2.0 A and 1.8 A resolution. Protein Sci. 1993 May;2(5):739–752. doi: 10.1002/pro.5560020506. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Germann U. A., Müller G., Hunziker P. E., Lerch K. Characterization of two allelic forms of Neurospora crassa laccase. Amino- and carboxyl-terminal processing of a precursor. J Biol Chem. 1988 Jan 15;263(2):885–896. [PubMed] [Google Scholar]
  13. Guss J. M., Freeman H. C. Structure of oxidized poplar plastocyanin at 1.6 A resolution. J Mol Biol. 1983 Sep 15;169(2):521–563. doi: 10.1016/s0022-2836(83)80064-3. [DOI] [PubMed] [Google Scholar]
  14. He S., Modi S., Bendall D. S., Gray J. C. The surface-exposed tyrosine residue Tyr83 of pea plastocyanin is involved in both binding and electron transfer reactions with cytochrome f. EMBO J. 1991 Dec;10(13):4011–4016. doi: 10.1002/j.1460-2075.1991.tb04976.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Hochkoeppler A., Zannoni D., Ciurli S., Meyer T. E., Cusanovich M. A., Tollin G. Kinetics of photo-induced electron transfer from high-potential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentans. Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):6998–7002. doi: 10.1073/pnas.93.14.6998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kawula T. H., Spinola S. M., Klapper D. G., Cannon J. G. Localization of a conserved epitope and an azurin-like domain in the H.8 protein of pathogenic Neisseria. Mol Microbiol. 1987 Sep;1(2):179–185. doi: 10.1111/j.1365-2958.1987.tb00510.x. [DOI] [PubMed] [Google Scholar]
  17. McManus J. D., Brune D. C., Han J., Sanders-Loehr J., Meyer T. E., Cusanovich M. A., Tollin G., Blankenship R. E. Isolation, characterization, and amino acid sequences of auracyanins, blue copper proteins from the green photosynthetic bacterium Chloroflexus aurantiacus. J Biol Chem. 1992 Apr 5;267(10):6531–6540. [PubMed] [Google Scholar]
  18. Meyer T. E., Zhao Z. G., Cusanovich M. A., Tollin G. Transient kinetics of electron transfer from a variety of c-type cytochromes to plastocyanin. Biochemistry. 1993 May 4;32(17):4552–4559. doi: 10.1021/bi00068a010. [DOI] [PubMed] [Google Scholar]
  19. Miyake S., Emori Y., Suzuki K. Gene organization of the small subunit of human calcium-activated neutral protease. Nucleic Acids Res. 1986 Nov 25;14(22):8805–8817. doi: 10.1093/nar/14.22.8805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Modi S., Nordling M., Lundberg L. G., Hansson O., Bendall D. S. Reactivity of cytochromes c and f with mutant forms of spinach plastocyanin. Biochim Biophys Acta. 1992 Aug 28;1102(1):85–90. doi: 10.1016/0005-2728(92)90068-d. [DOI] [PubMed] [Google Scholar]
  21. Murphy M. E., Lindley P. F., Adman E. T. Structural comparison of cupredoxin domains: domain recycling to construct proteins with novel functions. Protein Sci. 1997 Apr;6(4):761–770. doi: 10.1002/pro.5560060402. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Norris G. E., Anderson B. F., Baker E. N. Structure of azurin from Alcaligenes denitrificans at 2.5 A resolution. J Mol Biol. 1983 Apr 15;165(3):501–521. doi: 10.1016/s0022-2836(83)80216-2. [DOI] [PubMed] [Google Scholar]
  23. Rydén L. G., Hunt L. T. Evolution of protein complexity: the blue copper-containing oxidases and related proteins. J Mol Evol. 1993 Jan;36(1):41–66. doi: 10.1007/BF02407305. [DOI] [PubMed] [Google Scholar]
  24. Schubert W. D., Klukas O., Saenger W., Witt H. T., Fromme P., Krauss N. A common ancestor for oxygenic and anoxygenic photosynthetic systems: a comparison based on the structural model of photosystem I. J Mol Biol. 1998 Jul 10;280(2):297–314. doi: 10.1006/jmbi.1998.1824. [DOI] [PubMed] [Google Scholar]
  25. Van Beeumen J., Van Bun S., Canters G. W., Lommen A., Chothia C. The structural homology of amicyanin from Thiobacillus versutus to plant plastocyanins. J Biol Chem. 1991 Mar 15;266(8):4869–4877. [PubMed] [Google Scholar]
  26. Woese C. R. Bacterial evolution. Microbiol Rev. 1987 Jun;51(2):221–271. doi: 10.1128/mr.51.2.221-271.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Woese C. The universal ancestor. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6854–6859. doi: 10.1073/pnas.95.12.6854. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. van Spanning R. J., Wansell C. W., Reijnders W. N., Oltmann L. F., Stouthamer A. H. Mutagenesis of the gene encoding amicyanin of Paracoccus denitrificans and the resultant effect on methylamine oxidation. FEBS Lett. 1990 Nov 26;275(1-2):217–220. doi: 10.1016/0014-5793(90)81475-4. [DOI] [PubMed] [Google Scholar]

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