Titlebook: Bioenergetics; Energy Conservation Günter Schäfer,Harvey S. Penefsky Book 2008 Springer-Verlag Berlin Heidelberg 2008 ATP.ATP Formation.Ar

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https://doi.org/10.1007/978-3-8350-9315-7ive genomic analysis of microbial genomes and environmentalmetagenomes coupled with structural modelling to explore the diversity of aerobic respiration in Archaea.We focus on the heme–copper oxidoreductase superfamily which is responsible for catalyzing the terminalreaction in aerobic respiration—t

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https://doi.org/10.1007/978-3-8349-8925-3opsins has been considerably extended, not only in viewof the large number of family members, but also their functional properties as pumps, sensors, and channels.In this review, we give a short overview of old and newly discovered microbial rhodopsins, the mechanism of signal transfer and ion trans

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https://doi.org/10.1007/978-3-8349-8925-3ments such as rumen, anaerobic sediments of rivers andlakes, hyperthermal deep sea vents and even hypersaline environments. From an evolutionary standpoint theyare close to the origin of life. Common to all methanogens is the biological production of methane by a uniquepathway currently only found i

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https://doi.org/10.1007/978-3-8349-8195-0id anhydride bond to yield ADP and phosphate isutilized to drive various energy-consuming reactions. The ubiquitous F.F.ATP synthase produces the majority of ATP by converting the energy stored in a transmembrane electrochemicalgradient of H. or Na. into mechanical rotation. Whilethe mechanism of AT

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,Optionen für die Systemunterstützung, ⇆ 2H. + 2e.).Two metal atoms are present at their active center: either a Ni and an Fe atom in the [NiFe]hydrogenases,or two Fe atoms in the [FeFe]hydrogenases. They are phylogenetically distinct classes of proteins. Thecatalytic core of [NiFe]hydrogenases is a heterodimeric protein associated with

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