. Author manuscript; available in PMC: 2021 Mar 14.

Published in final edited form as: Nat Chem Biol. 2020 Sep 14;16(12):1434–1439. doi: 10.1038/s41589-020-0641-7

Table 1.

Photophysical properties of the selected fluorescent proteins.

	Chromophore-forming residues	Normal proteins				Proteins with aY-derived chromophores				Brightness ratios ^e
	Chromophore-forming residues	λ_ex ^a (nm)	λ_em ^b (nm)	ε (mM⁻¹ •cm⁻¹) ^c	φ ^d	λ_ex ^a (nm)	λ_em ^b (nm)	ε (mM⁻¹ •cm⁻¹) ^c	φ ^d	Brightness ratios ^e
sfGFP	TYG	485	510	85.6	0.70	541	605	125.1	0.43	89.8%
cpsGFP ^f	TYG	488	510	73.1	0.66	527	615	88.5	0.40	73.4%
mTFP1	AYG	462	492	65.6	0.81	514	581	85.5	0.50	80.5%
cpYFP ^g	GYG	503	515	76.3	0.58	569	609	82.6	0.38	70.9%
Citrine	GYG	516	529	75.3	0.75	565	624	95.0	0.45	75.7%

wavelength of the excitation peak.

wavelength of the emission peak.

extinction coefficient.

quantum yield.

molecular brightness (defined as ε×φ) of an aY-modified protein presented as the percentage of the molecular brightness of the corresponding normal protein.

circularly permuted sfGFP variant previously used to derive the hydrogen sulfide sensor, hsGFP.³³

circularly permuted EYFP variant previously used to derive the hydrogen sulfide sensor, cpGFP-pAzF.²³