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. 2019 Aug 27;20(17):4200. doi: 10.3390/ijms20174200

Table 4.

Redox GEFIs.

Name Analyte Permutant Sensor Unit λex,nm λem,nm Kd RA Reference
Peredox NADH/NAD+ cpT-Sapphire T-Rex 400/587 510/610 <5 nM for NADH for the first version P0 2.5-fold [70]
cpGFP-Tyr66pAzF H2S cpGFP Modified chromophore: UAAs are introduced 490 520 NM ≈ 3.5-fold [170]
hsGFP H2S cpsfGFP Modified chromophore: UAAs are introduced 454 500 H2S detection limit = 435 nM 23-fold [171]
pnGFP ONOO- cpsfGFP Modified chromophore: UAAs are introduced 484 508 ONOO- detection limit = 553 nM ≈ 25-fold [172]
NeonOxIrr H2O2 cpmNeonGreen OxyR 508 520 higher and similar sensitivity to low H2O2 concentra-tions, compared with HyPer-3 2.8-fold [173]
TriPer H2O2 cpYFP OxyR 405/488 NM NM NM [174]
HyPer H2O2 cpYFP OxyR 420/500 516 25 – 250 nM H2O2 detection (in vitro) 3-fold [90]
HyPer-2 H2O2 cpYFP OxyR 420/500 516 The same as for HyPer 6-fold [158]
HyPer-3 H2O2 cpYFP OxyR 420/500 516 The same as for HyPer 6-fold [105]
Frex NADH cpYFP B-Rex 420/500 518 3.7 μM 9-fold [99]
FrexH NADH cpYFP B-Rex 420/500 518 40 nM 3-fold [99]
RexYFP NADH/NAD+ cpYFP T-Rex 490 516 180 nM 2-fold [91]
SoNar NADH/NAD+ cpYFP T-Rex 420/485 528 0.2 μM for NADH
5.0 μM for NAD+ 		15-fold [81]
NAD+ sensor NAD+ cpVenus DNA ligase 405/488 ≈520 65 μM 2-fold [168]
iNap1 NADPH cpYFP T-Rex 420/500 515 2.0 μM 10-fold [100]
iNap2 NADPH cpYFP T-Rex 420/500 515 6.0 μM 10-fold [100]
iNap3 NADPH cpYFP T-Rex 420/500 515 25 μM 10-fold [100]
iNap4 NADPH cpYFP T-Rex 420/500 515 120 μM 10-fold [100]
Qser quinones cpYFP QsrR 427/496 515 NM 3.5-fold [169]
MetSOx S-MetO cpYFP MSRA and Trx1 425/505 510-516 K0.5 = 0.5 μM (in vitro) 6-fold [165]
MetROx MetO cpYFP MSRB and Trx3 410/500 510-516 K0.5 = 177 μM (in vitro) 6-fold [165]
OHSer ROOH cpVenus XcOhrR 519 526 NM 2-fold [164]
COSer CO cpVenus CooA 516 528 2 μM 2-fold [166]
HyPerRed H2O2 cpmApple OxyR 575 605 20 – 300 nM H2O2 detection (in vitro) 2-fold [103]
rxRFP general redox state cpmApple Redox sensitive peptides 576 600 NM 4-fold [175]

The raw colors refer to the colors of fluorescent proteins used as reporter domains. Kd—dissociation constant. NM—not measured. RA—response amplitude. UAA—unnatural amino acids.