Convergent Evolution of Cytochrome c6 and Plastocyanin
Cytochrome c6 and plastocyanin are an excellent case study of the convergent evolution of proteins. The two molecules differ in their primary sequence and 3D structure but function in a similar way to transfer electrons from cytochrome b 6 f to Photosystem I. It seems that cytochrome c6 was first “discovered” by Nature when iron was much more available than copper because of the reducing character of the Earth’s atmosphere. As the atmospheric molecular oxygen concentration began to rise because of photosynthetic activity, the relative bioavailabilities of iron and copper declined and rose, respectively, and cytochrome c6 was replaced with plastocyanin.
KeywordsFermentation Chlorophyll Ozone Respiration Proline
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- De la Cerda B, Díaz-Quintana A, Navarro JA, Hervás M and De la Rosa MA (1999) Site-directed mutagenesis of cytochrome c6 from Synechocystis sp. PCC 6803. The heme-protein possesses a negatively charged area that may be isofunctional with the acidic patch of plastocyanin. J Biol Chem 274: 13292–13297PubMedCrossRefGoogle Scholar
- De la Rosa MA, Navarro JA, Díaz-Quintana A, De la Cerda B, Molina-Heredia FP, Balme A, Murdoch PS, Díaz-Moreno I, Durán RV and Hervás M (2002) An evolutionary analysis of the reaction mechanisms of photosystem I reduction by cytochrome c6 and plastocyanin. Bioelectrochemistry 55: 41–45PubMedCrossRefGoogle Scholar
- Hong FT (2004) Molecular electronic switches in photobiology. In: Horspool W and Lenci F (eds) Handbook of Organic Photochemistry and Photobiology, 2nd Edition, Chapter 134. CRC Press, Boca RatonGoogle Scholar
- Kohzuma T, Inoue T, Yoshizaki F, Sasakawa Y, Onodera K, Nagatomo S, Kitagawa T, Uzawa S, Isobe Y, Sugimura Y, Gotowda M and Kai Y (1999) The structure and unusual pH dependence of plastocyanin from the fern Dryopteris crassirhizoma. The protonation of an active site histidine is hindered by π–π interactions. J Biol Chem 274: 11817–11823PubMedCrossRefGoogle Scholar
- Mathis P and Sétif P (1981) Near infra-red absorption spectra of the chlorophyll a cations and triplet state in vitro and in vivo. Isr J Chem 21: 316–320Google Scholar
- Metzger SU, Pakrasi HB and Whitmarsh J (1995) Characterization of a double deletion mutant that lacks cytochrome c6 and cytochrome cM in Synechocystis 6803. In: Mathis P (ed) Photosynthesis: From Light to Biosphere, pp 823–826. Kluwer Academic Publishers, DordrechtGoogle Scholar
- Molina-Heredia FP, Díaz-Quintana A, Hervás M, Navarro JA and De la Rosa MA (1999) Site-directed mutagenesis of cytochrome c6 from Nostoc species PCC 7119. Identification of surface residues of the hemeprotein involved in photosystem I reduction. J Biol Chem 274: 33565–33570PubMedCrossRefGoogle Scholar
- Navarro JA, Hervás M, Sun J, De la Cerda B, Chitnis PR and De la Rosa MA (2001a) Negatively charged residues in the H loop of PsaB subunit in photosystem I from Synechocystis sp. PCC 6803 appear to be responsible for electrostatic repulsions with plastocyanin. Photosynth Res 65: 63–68CrossRefGoogle Scholar
- Peschek G (1999) Photosynthesis and respiration of cyanobacteria. In: Peschek GA, Loeffelhord W and Schmetterer G (eds) The Phototrophic Prokaryotes, pp 201–209. Kluwer Academic/Plenum Publishers, New YorkGoogle Scholar
- Ullmann GM, Hauswald M, Jensen A, Kostic NM and Knapp E-W (1997) Comparison of the physiologically equivalent proteins cytochrome c6 and plastocyanin on the basis of their electrostatic potentials. Tryptophan 63 in cytochrome c6 may be isofunctional with tyrosine 83 in plastocyanin. Biochemistry 36: 16187–16196PubMedCrossRefGoogle Scholar
- Wastl J, Molina-Heredia FP, Hervás M, Navarro JA, De la Rosa MA, Bendall DS and Howe CJ (2004a) Redox properties of Arabidopsis cytochrome c6 are independent of the loop extension specific to higher plants. BBA-Bioenergetics 1657: 115–120Google Scholar
- Williams RJP and Fraústo da Silva JJR (1997) The Natural Selection of the Chemical Elements. Oxford University Press, OxfordGoogle Scholar