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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.
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
Luciferase is a generic term for the class of oxidative enzymes that produce bioluminescence, and is usually distinguished from a photoprotein.The name was first used by Raphaël Dubois who invented the words luciferin and luciferase, for the substrate and enzyme, respectively. [1]
The mobile water-soluble electron carrier is cytochrome c 6 in cyanobacteria, having been replaced by plastocyanin in plants. [8] Cyanobacteria can also synthesize ATP by oxidative phosphorylation, in the manner of other bacteria. The electron transport chain is NADH dehydrogenase → plastoquinol → b 6 f → cyt c 6 → cyt aa 3 → O 2
Peter D. Mitchell proposed the chemiosmotic hypothesis in 1961. [1] In brief, the hypothesis was that most adenosine triphosphate (ATP) synthesis in respiring cells comes from the electrochemical gradient across the inner membranes of mitochondria by using the energy of NADH and FADH 2 formed during the oxidative breakdown of energy-rich molecules such as glucose.
This word is taken from two Greek words, photos, which means light, and synthesis, which in chemistry means making a substance by combining simpler substances. So, in the presence of light, synthesis of food is called 'photosynthesis'. Noncyclic photophosphorylation through light-dependent reactions of photosynthesis at the thylakoid membrane.