Chapter 10 : Microaerobic Physiology: Aerobic Respiration, Anaerobic Respiration, and Carbon Dioxide Metabolism

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Microaerobic Physiology: Aerobic Respiration, Anaerobic Respiration, and Carbon Dioxide Metabolism, Page 1 of 2

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In aerobic respiration, electron transfer is to oxygen (more correctly, the dioxygen molecule), which is reduced to water with concomitant, coupled ion translocation and generation of an electrochemical gradient. In anaerobic respiration, electron transfer is to a molecule other than oxygen or to an ionic species, again coupled to generation of an electrochemical gradient. This chapter is concerned primarily with substrate oxidations and the use of oxygen as electron acceptor. It examines the evidence for facultative respiration in and considers the extent to which the respiratory pathways of this bacterium can be gleaned from the somewhat limited biochemical evidence presently available, and from comparisons with mitochondrial and bacterial paradigms. Oxidative stress responses are coordinated by a number of global regulatory proteins. In , alkylhydroperoxide reductase, catalase, and superoxide dismutase have been particularly implicated in the enzymatic destruction of toxic oxidants and are discussed in the chapter. is generally regarded as a microaerophile, but the bacterium also requires an elevated level of atmospheric CO for optimal growth.

Citation: Kelly D, Poole R, Hughes N. 2001. Microaerobic Physiology: Aerobic Respiration, Anaerobic Respiration, and Carbon Dioxide Metabolism, p 113-124. In Mobley H, Mendz G, Hazell S (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555818005.ch10

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Fatty Acid Biosynthesis
Sodium Dodecyl Sulfate
Reactive Oxygen Species
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Figure 1

Hypothetical arrangement of the major components of the respiratory chains of Reduced substrates (DH) are oxidized (to D) via membrane-bound or membrane-associated dehydrogenases. Integral membrane oxidoreductases include an NDH-1 complex (Nuo), the electron donor to which is unknown, and hydrogenase (Hya, also termed Hyd). Peripherally associated oxidoreductases include (among several others) malate:quinone oxidoreductase (Mqo). Reducing equivalents from all these substrates reduce the sole quinone, menaquinone-6, in the lipid bilayer of the inner membrane. Menaquinol reduces the trimeric cytochrome complex (Pet), which in turn reduces periplasmic cytochrome (). Cytochrome is reoxidized by the sole terminal oxidase of the Cco (or Fix) type, cytochrome (or ) Cytochrome may also be reoxidized by hydrogen peroxide in the periplasm through the activity of cytochrome peroxidase (CCP). Fumarate reductase (Frd) catalyzes electron transfer from menaquinol to fumarate as terminal acceptor. The reactions catalyzed by CcO, CCP, FrdA, Mqo, and Nuo show substrate/product conversions. The other arrows indicate directions of electron transfer.

Citation: Kelly D, Poole R, Hughes N. 2001. Microaerobic Physiology: Aerobic Respiration, Anaerobic Respiration, and Carbon Dioxide Metabolism, p 113-124. In Mobley H, Mendz G, Hazell S (ed), . ASM Press, Washington, DC. doi: 10.1128/9781555818005.ch10
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