Firefly luciferase catalyzes two sequential partial reactions resulting in the emission of light. The enzyme first catalyzes the adenylation of substrate luciferin with Mg-ATP followed by the multistep oxidation of the adenylate to form the light emitter oxyluciferin in an electronically excited state (PMID15683224).
|Residue in MACiE*||Atom in MACiE*||Residue Type in MACiE||Physiological
|MG(not in PDB) 1 x||MG||magnesium||magnesium||mononuclear|| Coordinates substrate|
*It refers to the MACiE reference pdb: 1ba3
|Metal/s Properties in Resting State|
|MG(not in PDB) 1 x||Resting state enzyme (-)|
|-Branchini BR, Southworth TL, Murtiashaw MH, Wilkinson SR, Khattak NF, Rosenberg JC, Zimmer M|
Mutagenesis evidence that the partial reactions of firefly bioluminescence are catalyzed by different conformations of the luciferase C-terminal domain.
Biochemistry. 2005 Feb 8;44(5):1385-93.(MEDLINE:15683224)
|-Nakatsu T, Ichiyama S, Hiratake J, Saldanha A, Kobashi N, Sakata K, Kato H, Nature. 2006 Mar 16;440(7082):285. |
Structural basis for the spectral difference in luciferase bioluminescence.
Nature. 2006 Mar 16;440(7082):372-6.(MEDLINE:16541080)