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ATP is quantified by measuring the light produced through its reaction with the naturally occurring firefly enzyme luciferase using a luminometer. The amount of light produced is directly proportional to the amount of ATP present in the sample. ATP tests can be used to: Control biological treatment reactors; Guide biocide dosing programs
The protein structure of firefly luciferase consists of 550 amino acids in two compact domains: the N-terminal domain and the C-terminal domain. The N-terminal domain is composed of two β-sheets in an αβαβα structure and a β barrel.
In 1848–49, Hippolyte Fizeau determined the speed of light using an intense light source at the bell tower of his father's holiday home in Suresnes, and a mirror 8,633 meters away on Montmartre. [2] The light source was interrupted by a rotating cogwheel with 720 notches that could be rotated at a variable speed several times a second.
[3] [4] [5] Thomas Young's experiment with light was part of classical physics long before the development of quantum mechanics and the concept of wave–particle duality. He believed it demonstrated that the Christiaan Huygens' wave theory of light was correct, and his experiment is sometimes referred to as Young's experiment [6] or Young's ...
The net reaction for the overall process of glycolysis is: [6] Glucose + 2 NAD+ + 2 P i + 2 ADP → 2 pyruvate + 2 ATP + 2 NADH + 2 H 2 O. Steps 1 and 3 require the input of energy derived from the hydrolysis of ATP to ADP and P i (inorganic phosphate), whereas steps 7 and 10 require the input of ADP, each yielding ATP. [7]
Unlike the modern double-slit experiment, Young's experiment reflects sunlight (using a steering mirror) through a small hole, and splits the thin beam in half using a paper card. [6] [10] [11] He also mentions the possibility of passing light through two slits in his description of the experiment: Modern illustration of the double-slit experiment