TY - JOUR
T1 - A comparative resonance raman analysis of heme-binding PAS domains
T2 - Heme iron coordination structures of the BjFixL, AxPDEA1, EcDoS, and MtDoS proteins
AU - Tomita, Takeshi
AU - Gonzalez, Gonzalo
AU - Chang, Alan L.
AU - Ikeda-Saito, Masao
AU - Gilles-Gonzalez, Marie Alda
PY - 2002/4/16
Y1 - 2002/4/16
N2 - The heme-PAS is a specialized domain with which a broad class of signal-transducing heme proteins detect physiological heme ligands. Such domains exhibit a wide range of ligand binding parameters, yet they are all expected to feature an α-β heme binding fold and a predominantly hydrophobic heme distal pocket without a distal histidine. We have compared, for the first time, the resonance Raman spectra of several heme-PASs: the heme-binding domains of Bradyrhizobium japonicum FixL, Escherichia coli Dos, Acetobacter xylinum PDEA1, and Methanobacterium thermoautotrophicum Dos. In all cases, the νFe-CO and νC-O values of the carbonmonoxy forms were consistent with coordination of the heme iron to histidine on the proximal side and binding of the CO without electrostatic interaction with the heme distal pocket. EcDos was unusual in having predominantly hexacoordinate heme iron in the deoxy and met forms. Despite an evident lack of CO interaction with the EcDos heme pocket, relatively low Fe-O2 (562 cm-1) and N-O (1576 cm-1) stretching frequencies indicated that strong polar interactions with that heme distal pocket are possible for highly bent ligands such as O2 or NO. None of the newly studied NO adducts exhibited evidence of the Fe-His rupture and pentacoordination previously noted for Sinorhizobium meliloti FixL. A low Fe-His stretching frequency, formerly interpreted as a strained Fe-His bond, and the slow association of O2 with S. meliloti FixL failed to correlate with the newly studied proteins having low association rate or low equilibrium association constants for binding of O2. We conclude that although heme-PASs share some features, they represent distinct signal transduction mechanisms.
AB - The heme-PAS is a specialized domain with which a broad class of signal-transducing heme proteins detect physiological heme ligands. Such domains exhibit a wide range of ligand binding parameters, yet they are all expected to feature an α-β heme binding fold and a predominantly hydrophobic heme distal pocket without a distal histidine. We have compared, for the first time, the resonance Raman spectra of several heme-PASs: the heme-binding domains of Bradyrhizobium japonicum FixL, Escherichia coli Dos, Acetobacter xylinum PDEA1, and Methanobacterium thermoautotrophicum Dos. In all cases, the νFe-CO and νC-O values of the carbonmonoxy forms were consistent with coordination of the heme iron to histidine on the proximal side and binding of the CO without electrostatic interaction with the heme distal pocket. EcDos was unusual in having predominantly hexacoordinate heme iron in the deoxy and met forms. Despite an evident lack of CO interaction with the EcDos heme pocket, relatively low Fe-O2 (562 cm-1) and N-O (1576 cm-1) stretching frequencies indicated that strong polar interactions with that heme distal pocket are possible for highly bent ligands such as O2 or NO. None of the newly studied NO adducts exhibited evidence of the Fe-His rupture and pentacoordination previously noted for Sinorhizobium meliloti FixL. A low Fe-His stretching frequency, formerly interpreted as a strained Fe-His bond, and the slow association of O2 with S. meliloti FixL failed to correlate with the newly studied proteins having low association rate or low equilibrium association constants for binding of O2. We conclude that although heme-PASs share some features, they represent distinct signal transduction mechanisms.
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U2 - 10.1021/bi0158831
DO - 10.1021/bi0158831
M3 - Article
C2 - 11939776
AN - SCOPUS:0037117726
SN - 0006-2960
VL - 41
SP - 4819
EP - 4826
JO - Biochemistry
JF - Biochemistry
IS - 15
ER -