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The Iron-Sulfur Centers and the Function of Hydrogenase from Clostridium Pasteurianum

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Book cover Iron and Copper Proteins

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 74))

Abstract

Hydrogenase has widespread occurrence among bacteria and algae. Its function allows the organisms to grow under some stringent conditions. In essence, activation of molecular hydrogen by hydrogenase (e.g., H2:NAD+ oxidoreductase EC 1.12.1.2; H2:ferricytochrome c3 oxidoreductase EC 1.12.2.1) enables the organisms to use H2 as the primary source of energy and/or reductant. Alternatively, production of H2 through hydrogenase (e.g., H2:ferredoxin oxidoreductase EC 1.12.7.1) permits the organism to use protons, perhaps the most available oxidant under anaerobic conditions, as the terminal electron acceptor to dispose of the excess electrons produced in oxidative metabolism. The latter is particularly important for obligate anaerobes such as Clostridium pasteurianum. A more detailed discussion on the physiological role of hydrogenase among microorganisms appeared recently (Mortenson and Chen, 1974).

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© 1976 Plenum Press, New York

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Chen, JS., Mortenson, L.E., Palmer, G. (1976). The Iron-Sulfur Centers and the Function of Hydrogenase from Clostridium Pasteurianum . In: Yasunodu, K.T., Mower, H.F., Hayaishi, O. (eds) Iron and Copper Proteins. Advances in Experimental Medicine and Biology, vol 74. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3270-1_6

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  • DOI: https://doi.org/10.1007/978-1-4684-3270-1_6

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-3272-5

  • Online ISBN: 978-1-4684-3270-1

  • eBook Packages: Springer Book Archive

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