1.1.2.4	2,6-dichlorophenolindophenol	can substitute for cytochrome c	287801, 389624, 389625, 389629, 389630	
1.1.2.4	cytochrome c	-	287801, 389624, 389626, 743861	
1.1.2.4	cytochrome c	cytochome c from horse-, beef- and tuna-heart more active than yeast cytochome c	389623	
1.1.2.4	cytochrome c	evaluation of the role of cytochrome c in D-lactate and methylglyoxal degradation. Recombinant expression of CYTC-1 in either the wild-type or cytc mutant background leads to increased tolerance to toxic concentrations of D-lactate and to a lesser extent also to methylglyoxal	743500	
1.1.2.4	cytochrome c	highly specific	389625	
1.1.2.4	cytochrome c	only cytochrome c-553 from same organism, eucaryotic cytochromes are not reduced	389630	
1.1.2.4	FAD	-	287801, 389623, 389624, 389625, 389626, 389629, 655064, 672323, 698932	
1.1.2.4	FAD	1 FAD per subunit	389628	
1.1.2.4	FAD	bound to the FAD binding domain of the enzyme	672749	
1.1.2.4	FAD	the enzyme is a flavoprotein. The flavin/pyridine cofactor redox state is detected fluorimetrically in cell homogenates	740447	
1.1.2.4	ferricytochrome c	-	740447	
1.1.2.4	FMN	-	672323	
1.1.2.4	additional information	no activity with NAD+ or NADP+	389626, 389630	
1.1.2.4	additional information	no activity with NAD+ or NADP+ as electron acceptors	698932	
1.1.2.4	additional information	ubiquinone and its associated dehydrogenase systems do not serve as electron acceptors and are upstream of the entry site of D-LDH-derived electrons into the electron transport chain	743500	
1.1.2.4	phenazine methosulfate	can substitute for cytochrome c	287801, 389623, 389625, 389630