1.7.7.1	C514S	almost complete loss of activity	394417	
1.7.7.1	C518S	almost complete loss of activity	394417	
1.7.7.1	G212S/L213T/Y214L/S217C/C220I/S221N	mutations mimic partially isoform SiRA	-, 742810	
1.7.7.1	G513A	increased Km for nitrite compared to the wild type enzyme	394417	
1.7.7.1	G513E	loss of most of the activity	394417	
1.7.7.1	G513V	loss of most of the activity	394417	
1.7.7.1	G519A	68% activity of wild type enzyme	394417	
1.7.7.1	G519E	8% activity of wild type enzyme	394417	
1.7.7.1	G519V	9% activity of wild type enzyme	394417	
1.7.7.1	K449Q	mutation does not affect enzymatic activity	726450	
1.7.7.1	M175E	the conformation of the Gln47 and Lys91 side-chains changes significantly. Compared with the conformation in wild-type, the Gln47 side-chain rotates about 120 degrees and the amino group in the Lys91 side-chain moves toward the side-chain of residue 175	726450	
1.7.7.1	M175G	the conformation of the Gln47 and Lys91 side-chains changes significantly. Compared with the conformation in wild-type, the Gln47 side-chain rotates about 120 degrees and the amino group in the Lys91 side-chain moves toward the side-chain of residue 175	726450	
1.7.7.1	M175K	the conformation of the Gln47 and Lys91 side-chains changes significantly. Compared with the conformation in wild-type, the Gln47 side-chain rotates about 120 degrees and the amino group in the Lys91 side-chain moves toward the side-chain of residue 175	726450	
1.7.7.1	additional information	various mutants that differ in enzymatic activity	394419	
1.7.7.1	P515A	marginal loss of activity	394417	
1.7.7.1	P515S	marginal loss of activity	394417	
1.7.7.1	P515T	marginal loss of activity	394417	
1.7.7.1	Q448K	mutation had only a negligible effect on the overall fold of the protein. In addition, the mutation did not affect the hydrogen bond interaction at the distal position of the siroheme	726450	
1.7.7.1	S217C	mutation mimics the corresponding residue in isoform SiRA, recovers sulfite reduction activity	-, 742810