| Literature DB >> 15547976 |
Takehiro Ohta1, Hideaki Yoshimura, Shiro Yoshioka, Shigetoshi Aono, Teizo Kitagawa.
Abstract
Resonance Raman (RR) evidence for structural linkage between the distal side of heme pocket and the signaling domain of an oxygen sensing hemoprotein, HemAT-Bs, is reported. The band-fitting analyses of the RR spectra in the Fe-O2 stretching (nuFe-O2) region revealed the presence of three conformers with nuFe-O2 at 554, 566, and 572 cm-1, which reflect different H-bond strengths on the bound O2 molecule. While recent X-ray analysis for CN--bound HemAT-Bs suggested the importance of Thr95 and Tyr70, the species with the strongest H-bond (554 cm-1) was deleted in the T95A mutant and also by removal of the linker and signal domains; however, the Y70F mutant maintained the same three conformers. A scheme for specific O2 sensing and signaling mechanism is discussed.Entities:
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Year: 2004 PMID： 15547976 DOI： 10.1021/ja046896f
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419