Abstract:
:2-Oxoacid:ferredoxin oxidoreductases (OFORs) are essential enzymes in microbial one-carbon metabolism. They use thiamine pyrophosphate to reversibly cleave carbon-carbon bonds, generating low potential (∼-500mV) electrons. Crystallographic analysis of a recently discovered OFOR, an oxalate oxidoreductase (OOR), has provided a second view of OFOR architecture and active site composition. Using these recent structural data along with the previously determined structures of pyruvate:ferredoxin oxidoreductase, structure-function relationships in this superfamily have been expanded and re-evaluated. Additionally, structural motifs have been defined that better serve to distinguish one OFOR subfamily from another and potentially uncover novel OFORs.
journal_name
Curr Opin Struct Bioljournal_title
Current opinion in structural biologyauthors
Gibson MI,Chen PY,Drennan CLdoi
10.1016/j.sbi.2016.05.011subject
Has Abstractpub_date
2016-12-01 00:00:00pages
54-61eissn
0959-440Xissn
1879-033Xpii
S0959-440X(16)30046-Xjournal_volume
41pub_type
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