Abstract：
:Electronic absorption, EPR, and resonance Raman spectroscopies revealed that CooA, the CO-sensing transcriptional regulator from Rhodospirillum rubrum, reacts with NO to form a five-coordinate NO-heme. NO must therefore displace both of the heme ligands from six-coordinate, low-spin Fe(II)CooA in forming five-coordinate Fe(II)CooA(NO). CO, in contrast, displaces a single heme ligand from Fe(II)CooA to form six-coordinate Fe(II)CooA(CO). Of a series of common heme-binding ligands, only CO and NO were able to bind to the heme of wild-type CooA; imidazole, azide anion, and cyanide anion had no effect on the heme absorption spectrum. Although NO binds to the heme and displaces the endogenous ligands, NO was not able to induce CooA to bind to its target DNA. The mechanism of CO-dependent activation of CooA is thus more complex than simple displacement of a ligand from the heme iron since NO does not trigger DNA binding. These observations suggest that the CooA heme site discriminates between NO and the biologically relevant signal, CO.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Reynolds MF,Parks RB,Burstyn JN,Shelver D,Thorsteinsson MV,Kerby RL,Roberts GP,Vogel KM,Spiro TGdoi
10.1021/bi991378gsubject
Has Abstractpub_date
2000-01-18 00:00:00pages
388-96issue
2eissn
0006-2960issn
1520-4995pii
bi991378gjournal_volume
39pub_type
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