Structural and Functional Characterization of the Globin-Coupled Sensors ofAzotobacter vinelandiiandBordetella pertussis

Abstract

Antioxidants and Redox SignalingStructural and functional characterization of the globin-coupled sensors of Azotobacter vinelandii and Bordetella pertussis

Structural modeling of a novel membrane-bound globin-coupled sensor in Geobacter sulfurreducens

“…S2 ). Furthermore, the crystal structure obtained for the GD of Gs GCS is comparable with those from Ec DosC [12] and Bp GReg [17] , [46] which further supports the GCS-like character of the globin folded structure in Gs GCS [16] .…”

“…Despite some progress over the last decade, our knowledge of GCS ( Table S1 ) is predominantly limited to individual domains ( Table S2 ), while a more comprehensive view of the structure and the intramolecular signal transduction of the full-length protein is lacking, unsurprisingly, as there is no structure of a full-length GCS available today. Crystal structures are largely limited to the globin domain only [12] , [15] , [16] , [17] or to each domain individually, e.g. for ( Ec DosC) [12] .…”

Resonance Raman studies of gas sensing heme proteins

“…[58,79] Several other amino acid residues in the heme distal pocket are essential in stabilization of the O 2 -heme complex of FixL, their roles being elucidated by systematically conducting rR spectroscopy on judicially engineered site-directed mutants. Specifically, Mukai and coworkers examined the roles of Ile209 and Ile210 residues that are located Fe(III) 1370 1492 1562 6cLS [48] EcDOS Fe(II) 1362 1494 1581 6cLS [56] Fe(III) 1371 1506 1578 6cLS [56] HemAT-Bs YddV Fe(II) 1352 1469 1558 5cHS [67] Fe(III) 1370 1495 1568 5cHS [68] Fe(II) 1353 1470 1564 5cHS [68] AvGReg Fe(II) 1375 1506 1588 6cLS [69] Fe(II) 1357 1474 1567 5cHS [70] BpeGReg CooA Fe(II) 1357 1472 1565 5cHS [70] Fe(III) 1375 1504 1582 6cLS [71] Fe(II) 1361 1492 1580 6cHS [71] sGC Fe(II) 1358 1471 1562 5cHS [72] Tt HNOX Fe(II) 1354 1471 1575 5cHS [73] Vc HNOX Fe(II) 1354 1471 1561 5cHS [73] Note: 5cHS (five-coordinated high spin); 6cLS (six-coordinated low spin).…”

“…Other typical examples of GCS proteins with diguanylate cyclase activity have also been identified in Azotobacter vinelandii (AvGreg), [69] Bordetella pertussis (BpeGReg) [119][120][121][122] Desulfotalea psychrophia (HemDGC), [138] T A B L E 2 Heme skeletal vibrations and vibrational modes of Fe-XY ligands in various heme proteins Pectobacterium carotovorum (PccGCS) [122] Shewanella putrefaciens (SpDosD), [123] etc. The rR data for AvGreg and BpeGReg were recorded in the deoxy and oxy state, [70] where the frequencies are summarized in Table 1 and Table 2. The ferrous forms of both proteins have a five-coordinated high spin heme, the ν(Fe-N his ) being observed at 227 and 229 cm À1 , respectively.…”

“…FixL* and FixLN 212 [45] HemAT-Bs 225 [67] YddV wild-type 227 [68] YddV Y43F 227 [68] AvGReg 227 [70] BpeGReg 229 [70] HemDGC 226 [138] Mb 220 [4,77] sGC 204 [72] Vc H-NOX 224 [73] Tt H-NOX 218 [73] binding of NO, with its well-known trans-effect, [78,146] results in a five-coordinated NO complex by breaking the iron histidine bond, [147] as confirmed by the rR spectra exhibiting features characteristic of a five coordinated heme, where the ν(Fe-N) and ν(N-O) stretching modes were observed at 525 and 1677 cm À1 , respectively. [72] Understandably, the cleavage of the iron histidine bond has been proposed to be a key step inducing the protein conformational change that is propagated to the remote catalytic site.…”