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Most useful ATP analogs cannot be hydrolyzed as ATP would be; instead, they trap the enzyme in a structure closely related to the ATP-bound state. Adenosine 5′-(γ-thiotriphosphate) is an extremely common ATP analog in which one of the gamma-phosphate oxygens is replaced by a sulfur atom; this anion is hydrolyzed at a dramatically slower rate ...
The driving force is due to the ATP (−4) having a more negative charge than the ADP (−3), and thus it dissipates some of the electrical component of the proton electrochemical gradient. The outcome of these transport processes using the proton electrochemical gradient is that more than 3 H + are needed to make 1 ATP.
Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exchange medium in the cell. During aerobic respiration, ATP is synthesized in the mitochondrion by addition of a third phosphate group to adenosine diphosphate (ADP) in a ...
There are two types of active transport: primary active transport that uses adenosine triphosphate (ATP), and secondary active transport that uses an electrochemical gradient. This process is in contrast to passive transport , which allows molecules or ions to move down their concentration gradient, from an area of high concentration to an area ...
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ATP synthase is an enzyme that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (P i). ATP synthase is a molecular machine .
A facultative anaerobic organism is an organism that makes ATP by aerobic respiration if oxygen is present, but is capable of switching to fermentation if oxygen is absent. [1] [2] Some examples of facultatively anaerobic bacteria are Staphylococcus spp., [3] Escherichia coli, Salmonella, Listeria spp., [4] Shewanella oneidensis and Yersinia ...
The ATP molecule binds to the connecting point of each subunit of the dimer, indicating that ATP is in close proximity to both subunits during catalysis. The two binding motifs that ATP directly interacts with is the residues from the Walker A motif, located on one of the subunits, and the residues from the C binding motif, located on the other ...