Sandbox GGC3: Difference between revisions
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The first partial reaction entails the conversion of the carboxyl group of <small>D</small>-luciferin<ref name="Sundlov"/><ref name="Bruce">Branchini, B. R., Southworth, T. L., Murtiahsaw, M. H., Wilkinson, S. R., Khattak, N. F., Rosenberg, J. C., & Zimmer, M. (2005). Mutagenesis Evidence that the Partial Reactions of Firefly Bioluminescence are Catalyzed by Different Conformations of the Luciferase C-Terminal Domain. “Biochemistry 44”(5), 1385-1393. https://doi.org/10.1021/bi047903f</ref><ref name="Nakamura">Nakamura, M., Maki, S., Amano, Y., Ohkita, Y., Niwa, K., Hirano, T., Ohmiya, Y., & Niwa, H. (2005). Firefly luciferase exhibits bimodal action depending on the luciferin chirality. “Biochemical and Biophysical Research Communications, 331”(2), 471–475. https://doi.org/10.1016/j.bbrc.2005.03.202</ref> by luciferase in the presence of ATP and Mg<sup>2+</sup>, yielding luciferyl-adenylate (LH<sub>2</sub>-AMP) and pyrophosphate as a by-product. Amino acid residues subsequently are recruited to promote the oxidation of LH<sub>2</sub>-AMP using molecular oxygen by luciferase (acting as a monooxygenase)<ref name="Oba">Oba, Y., Ojika, M., Inouye, S. (2003). Firefly luciferase is a bifunctional enzyme: ATP-dependent monoxygenase and a long chain fatty acyl-CoA synthetase. “FEBS Letters 540”(1-3), 251-254. https://doi.org/10.1016/S0014-5793(03)00272-2</ref>, which then eventually yields oxyluciferin in the excited-state and CO<sub>2</sub>. It is upon the return from the excited-state to the ground state that the emittance of a yellow-green light is observed (λ≈560 nm)<ref name=Nakamura/>. | The first partial reaction entails the conversion of the carboxyl group of <small>D</small>-luciferin<ref name="Sundlov"/><ref name="Bruce">Branchini, B. R., Southworth, T. L., Murtiahsaw, M. H., Wilkinson, S. R., Khattak, N. F., Rosenberg, J. C., & Zimmer, M. (2005). Mutagenesis Evidence that the Partial Reactions of Firefly Bioluminescence are Catalyzed by Different Conformations of the Luciferase C-Terminal Domain. “Biochemistry 44”(5), 1385-1393. https://doi.org/10.1021/bi047903f</ref><ref name="Nakamura">Nakamura, M., Maki, S., Amano, Y., Ohkita, Y., Niwa, K., Hirano, T., Ohmiya, Y., & Niwa, H. (2005). Firefly luciferase exhibits bimodal action depending on the luciferin chirality. “Biochemical and Biophysical Research Communications, 331”(2), 471–475. https://doi.org/10.1016/j.bbrc.2005.03.202</ref> by luciferase in the presence of ATP and Mg<sup>2+</sup>, yielding luciferyl-adenylate (LH<sub>2</sub>-AMP) and pyrophosphate as a by-product. Amino acid residues subsequently are recruited to promote the oxidation of LH<sub>2</sub>-AMP using molecular oxygen by luciferase (acting as a monooxygenase)<ref name="Oba">Oba, Y., Ojika, M., Inouye, S. (2003). Firefly luciferase is a bifunctional enzyme: ATP-dependent monoxygenase and a long chain fatty acyl-CoA synthetase. “FEBS Letters 540”(1-3), 251-254. https://doi.org/10.1016/S0014-5793(03)00272-2</ref>, which then eventually yields oxyluciferin in the excited-state and CO<sub>2</sub>. It is upon the return from the excited-state to the ground state that the emittance of a yellow-green light is observed (λ≈560 nm)<ref name=Nakamura/>. | ||
