Fluorescent ATP Analogues page

Thanks to Clive Bagshaw who collated this information. Show/Hide structures

Analogue
Structure
Absorption max (nm)
Emission max (nm)
Quantum yield
Fluorecence lifetime (ns)
rf
e-ATP
275 (310)
415
0.59
26
0.9x
e-aza-ATP
354 (365)
484
-
-
3
FTP
295 (313)
340
0.054
< 1
5
2AP-TP
303
370
0.063
7
0.95
TNP-ATP
408 470
540
-
-
y
ant-ATP
332
428
0.14
-
-
mant-ATP
350
446
0.22
4
2.5
DEDA-ATP
330
578
0.089
3.6
3.2
FEDA-ATP
495 (436)
520
0.9
4.2
0.4
REDA-ATP
553 (546)
580
0.3
1.7
0.55
Cy3-EDA-ATP
552
568
0.03
1.3
Cy5-EDA-ATP
648
665
0.1
-
0.93
DTP
320
534
-
-
1.6

(a) Secrist et al., 1972; (b) Rosenfeld and Taylor, 1984; (c) Miyata and Asai, 1982; (d) Smith and White, 1985a; (e) Ward et al., 1966a; (f) Jackson and Bagshaw, 1988; (g) Bagshaw, 1974; (h) Hiratsuka and Uchida, 1973; (i) Hiratsuka, 1983; (j) Cremo et al., 1990; (k) Conibear et al., 1996; (l) Chang and Cheung, 1992; (m) Mujumdar et al., 1993; (n) Onodera and Yagi, 1971. (x) a fluorescence enhancement seen if e-ATP is excited via tryptophan or free e-ATP is quenched with acrylamide. (y) a large enhancement observed when TNP-ATP binds to secondary site

Absorption (excitation) and emission wavelengths, molar absorption coefficients, quantum yield and fluorescence lifetime are given for the free fluorophores in aqueous solvents (at pH 7.0 where available). Values in brackets refer to recommended (non-peak) settings to avoid overlapping protein absorbtion and/or to match the output from a Hg arc lamp.

RF represents the fluorescence of the nucleotide when bound to myosin as its predominant steady-state intermediate or trapped form relative to the fluorescence of the free nucleotide. These numbers are approximate because they depend on the bandwidth of the emission detector relative to any accompanying spectral shifts, as well as on solvent conditions.