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Soluble Electron Transfer Catalysts of Cyanobacteria

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The Molecular Biology of Cyanobacteria

Part of the book series: Advances in Photosynthesis ((AIPH,volume 1))

Summary

This review covers only a fraction of the area of one written a dozen years ago on photosynthesis in cyanobacteria (Ho and Krogmann, 1982) yet it cites many more references than that earlier work. The power of reductionist laboratory science has increased immensely in the intervening years. The soluble electron transfer catalysts of photosynthesis have received disproportionate attention since soluble proteins are more easily dealt with by the techniques of protein chemistry. Research on each of the catalysts reviewed here has exposed a variety of insights through the tools of contemporary science. The many studies of different forms of ferredoxin in cyanobacteria promise new understanding of the regulation of electron transfer and its mechanism. The crystal structures of ferredoxin, ferredoxin-NADP+ oxidoreductase, flavodoxin and plastocyanin are elegant examples of what our broader understanding will become. The powerful technique of gene deletion used on cytochrome c 6 (cytochrome c 553) has done more than confirm preconceptions. It has given us the intriguing puzzle of why more than two routes of electron flow between carriers of very similar redox potential may be used. The low potential cytochrome c beckons for an explanation of its catalytic function and for an understanding of its role in the ancient origin of other cytochromes. Finally, hydrogenase, whose catalytic act is the simplest—the movement of an electron to or from a proton—seems ready for understanding. Hydrogenase has a long history of fragility and activity loss during purification. One type of hydrogenase has now been purified and there are glimpses of its metabolic role.

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Morand, L.Z., Cheng, R.H., Krogmann, D.W., Ho, K.K. (1994). Soluble Electron Transfer Catalysts of Cyanobacteria. In: Bryant, D.A. (eds) The Molecular Biology of Cyanobacteria. Advances in Photosynthesis, vol 1. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-0227-8_12

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