1.14.99.58	F117Y	no change in regioselectivity	661923	
1.14.99.58	F189A	the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin	742737	
1.14.99.58	F189G	the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin	742737	
1.14.99.58	F189L	the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin	742737	
1.14.99.58	F189T	the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin	742737	
1.14.99.58	G125V	single-phase kinetics of transfer of heme from heme-binding protein PhuS	678146	
1.14.99.58	H26A/K34A/K132A	inactive	742894	
1.14.99.58	K132A	the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 12% of alpha-biliverdin in addition to the formation of normal beta- (26%) and delta- (62%) biliverdins	742737	
1.14.99.58	K34A	the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 11% of alpha-biliverdin in addition to the formation of normal beta- (34%) and delta- (55%) biliverdins	742737	
1.14.99.58	K34A/K132A	the heme degradation activity of the mutant is similar to that of the wild-type enzyme, but the mutant produces 18% of alpha-biliverdin in addition to the formation of normal beta- (27%) and delta- (56%) biliverdins	742737	
1.14.99.58	additional information	chromosomal knock-out gene bphO mutants shows identical growth behavior as the wild type under various conditions, the bphO mutant and the double mutant strain DELTAbphO show increased levels of pyocyanin, as well as decreased heat tolerance in the stationary phase, phenotypes, overview	692400	
1.14.99.58	N19K	no change in regioselectivity	661923	
1.14.99.58	N19K/F117Y	change in regioselectivity, producing alpha-biliverdin and less beta- and delta-biliverdin, enzyme exists as a mixture of molecules exhibiting 2 distinct heme seatings, one seating is identical to wild-type, the other is similar to that typical of alpha-hydroxylating heme oxigenases	661923	
1.14.99.58	N19K/F117Y	destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics	678146	
1.14.99.58	N19K/F117Y/K132A	destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics	678146	
1.14.99.58	N19K/F117Y/K34N	destabilization of heme within the protein, transfer of heme from heme binding protein PhuS is not affected and shows biphasic kinetics	678146	
1.14.99.58	N19K/K34A/F117Y/K132A	the mutant produces biliverdin-IX-alpha	742894	
1.14.99.58	R80L	mutant exhibits allmost global conformational disorder related to significantly lower efficiency to hydroxylate heme in the presence of H2O2	680357	
1.14.99.58	T189W	the heme degradation activity of the mutant is similar to that of the wild-type enzyme. The mutant produces only beta- and delta-biliverdins, but no alpha-biliverdin	742737