The methylamine dehydrogenase electron transfer chain

C. Dennison, G.W. Canters, S. de Vries, E. Vijgenboom, R.J.M. van Spanning

    Research output: Contribution to JournalReview articleAcademicpeer-review

    Abstract

    This chapter discusses the methylamine dehydrogenase electron transfer chain. Mitochondiral respiration is attractive because of its relatively uncomplicated organization. The respiratory chain consists of a single sequence of redox proteins with only two possible substrates and a single terminal electron acceptor. The simplicity of the mitochondria1 respiratory apparatus belies its evolutionary origin. During respiration, cellular redox free energy is converted into chemic-osmotic and chemical energy. The conversion is mediated by the flow of electrons, which, in an oxidizing environment, run from low to high potential. In bacteria, the reducing equivalents may be derived from a variety of sources, such as sulfur or nitrogen in low oxidation states (S, S2-, NH3), molecular hydrogen, or even ferrous ions. Terminal electron acceptors may be provided by molecular oxygen, or by sulfur and nitrogen in high oxidation states—for example, SO42-, NO2-, and NO3-. The chain is similar to the methylamine dehydrogenase chain of Paracoccus denitrificans, and the results of the P. versutus studies can be compared with the P. denitrificans data where appropriate.
    Original languageEnglish
    Pages (from-to)351-407
    Number of pages57
    JournalAdvances in Inorganic Chemistry
    Volume45
    DOIs
    Publication statusPublished - 1998

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