Table 1.

Comparison of AidB with previously reported ACAD reduction potentials in mV. Measurements are listed for free enzymes as well as proteins in the presence of substrate (S), product (P), or non-optimal substrates described in the text or corresponding references.

Protein	Emox/sq	Emsq/red	Emox/red	% sq	pH	Radical	Ref.
AidB (300 mM NaCl)	−103	−258	−181	92	8.0	anionic	-
AidB + IVCoA (300 mM NaCl)	−148	−297	−222	91	8.0	anionic	-
AidB (100 mM NaCl)	−160	−315	−237	92	8.0	anionic	-
AidB + pUC19 (100 mM NaCl)	−121	−274	−197	92	8.0	anionic	-
AidB + 28-mer (100 mM NaCl)	−129	−282	−205	92	8.0	anionic	-
MeSCAD	-	-	−79	5	7.0	neutral	[35]
MeSCAD + S/P	-	-	−19	0	7.0	-	[37]
MeSCAD + Butyl-CoA	-	-	−79	0	6.9	-	[36]
MeSCAD + Acetoacetyl-CoA	-	-	−180	0	7.0	-	[35]
PdGCD	-	-	−85	0	6.4	-	[39]
PdGCD + S/P	-	-	30	5	6.4	anionic	[39]
PdGCD + Acetoacetyl-CoA	−154 †	−104 †	−129	15	6.4	neutral	[39]
pMCAD	−166	−129	−136	20	7.6	neutral	[38]
pMCAD + S/P	-	-	−26	0	7.6	-	[34]
pMCAD + Butyl-CoA	−189 †	−155 †	−172	20	7.6	neutral	[38]
hSCAD *	-	-	−141	≤5	7.6	-	[40]
hSCAD * + Butyryl-CoA	-	-	−103	≤5	7.6	-	[40]
hSCAD * + Octanoyl-CoA	-	-	−161	≤5	7.6	-	[40]

^*hSCAD reduction potentials reported for inactivated mutant enzyme.

^†Values calculated from reported E_m and percent semiquinone values.