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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Electrons
Sulfur
Nitrogen
Oxidation
Molecular oxygen
Free energy
Hydrogen
Bacteria
Ions
methylamine dehydrogenase
Substrates
Proteins
Oxidation-Reduction
Electron Transport

Cite this

Dennison, C. ; Canters, G.W. ; de Vries, S. ; Vijgenboom, E. ; van Spanning, R.J.M. / The methylamine dehydrogenase electron transfer chain. In: Advances in Inorganic Chemistry. 1998 ; Vol. 45. pp. 351-407.
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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.",
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The methylamine dehydrogenase electron transfer chain. / Dennison, C.; Canters, G.W.; de Vries, S.; Vijgenboom, E.; van Spanning, R.J.M.

In: Advances in Inorganic Chemistry, Vol. 45, 1998, p. 351-407.

Research output: Contribution to JournalReview articleAcademicpeer-review

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AB - 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.

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